Publications

Blum, T. B., Housset, D., Clabbers, M. T. B., van Genderen, E., Bacia-Verloop, M., Zander, U., McCarthy, A. A., Schoehn, G., Ling, W. L. and Abrahams, J. P. (2021) “Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals”, Acta Crystallographica Section D, 77(1), pp. 75–85. doi: 10.1107/S2059798320014540, multiple elastic (or dynamical) scattering, which is prominent in electron diffraction, is a concern. Current methods for modeling dynamical scattering by multi-slice or Bloch wave approaches are not suitable for protein crystal.   
Thakkar, P., Guzenko, V. A., Lu, P.-H., Dunin-Borkowski, R. E., Abrahams, J. P. and Tsujino, S. (2020) “Fabrication of low aspect ratio three-element Boersch phase shifters for voltage-controlled three electron beam interference”, Journal of Applied Physics. AIP Publishing, 128(13), p. 134502. doi: 10.1063/5.0020383.   edoc
Merg, A. D., Touponse, G., van Genderen, E., Blum, T. B., Zuo, X., Bazrafshan, A., Siaw, H. M. H., McCanna, A., Dyer, R. B., Salaita, K., Abrahams, J. P. and Conticello, V. P. (2020) “Shape-Shifting Peptide Nanomaterials: Surface Asymmetry Enables pH-Dependent Formation and Interconversion of Collagen Tubes and Sheets”, Journal of the American Chemical Society. American Chemical Society, 142(47), pp. 19956–19968. doi: 10.1021/jacs.0c08174.   edoc
Xiao, X., Elsayed, S. S., Wu, C., van der Heul, H. U., Metsä-Ketelä, M., Du, C., Prota, A. E., Chen, C.-C., Liu, W., Guo, R.-T., Abrahams, J. P. and van Wezel, G. P. (2020) “Functional and Structural Insights into a Novel Promiscuous Ketoreductase of the Lugdunomycin Biosynthetic Pathway”, ACS Chemical Biology. American Chemical Society, 15(9), pp. 2529–2538. doi: 10.1021/acschembio.0c00564.   edoc | Open Access
van Schayck, J. P., van Genderen, E., Maddox, E., Roussel, L., Boulanger, H., Fröjdh, E., Abrahams, J.-P., Peters, P. J. and Ravelli, R. B. G. (2020) “Sub-pixel electron detection using a convolutional neural network”, Ultramicroscopy. Elsevier, 218, p. 113091. doi: 10.1016/j.ultramic.2020.113091.   edoc
Matz, J. M., Drepper, B., Blum, T. B., van Genderen, E., Burrell, A., Martin, P., Stach, T., Collinson, L. M., Abrahams, J. P., Matuschewski, K. and Blackman, M. J. (2020) “A lipocalin mediates unidirectional heme biomineralization in malaria parasites”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 117(28), pp. 16546–16556. doi: 10.1073/pnas.2001153117.   edoc | Open Access
Zhang, Z., Wen, K., Zhang, C., Laroche, F., Wang, Z., Zhou, Q., Liu, Z., Abrahams, J. P. and Zhou, X. (2020) “Extracellular Nanovesicle Enhanced Gene Transfection Using Polyethyleneimine in HEK293T Cells and Zebrafish Embryos”, Frontiers in Bioengineering and Biotechnology. Frontiers Media, 8, p. 448. doi: 10.3389/fbioe.2020.00448.   edoc | Open Access
Blum, T. B., Housset, D., Clabbers, M. T. B., van Genderen, E., Bacia-Verloop, M., Zander, U., McCarthy, A. A., Schoehn, G., Li Ling, W. and Abrahams, J. P. (2020) “Statistically correcting dynamical electron scattering improves refinement of protein nanocrystals, including charge refinement of coordinated metals”, bioRxiv. Cold Spring Harbor Laboratory, p. https://doi.org/10.1101/2020.07.08.191049. doi: 10.1101/2020.07.08.191049.   
Wallin, C., Hiruma, Y., Warmlander, S., Huvent, I., Jarvet, J., Abrahams, J. P., Graslund, A., Lippens, G. and Luo, J. (2019) “The Neuronal Tau Protein Blocks In Vitro Fibrillation of the Amyloid-beta (A beta) Peptide”, Biophysical Journal. CellPress. doi: 10.1016/j.bpj.2018.11.1657.   edoc
Blum, T. B. and Abrahams, J. P. (2019) “6T17: Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia”, Worldwide Protein Data Bank, p. 6T17. doi: 10.2210/pdb6t17/pdb.   edoc
Gemmi, M., Mugnaioli, E., Gorelik, T. E., Kolb, U., Palatinus, L., Boullay, P., Hovmöller, S. and Abrahams, J. P. (2019) “3D Electron Diffraction: The Nanocrystallography Revolution”, ACS central science, 5(8), pp. 1315–1329. doi: 10.1021/acscentsci.9b00394.   edoc
Merg, A. D., Touponse, G., van Genderen, E., Zuo, X., Bazrafshan, A., Blum, T., Hughes, S., Salaita, K., Abrahams, J. P. and Conticello, V. P. (2019) “2D Crystal Engineering of Nanosheets Assembled from Helical Peptide Building Blocks”, Angewandte Chemie (International ed. in English), 58(38), pp. 13507–13512. doi: 10.1002/anie.201906214.   edoc
Clabbers, M. T. B., Gruene, T., van Genderen, E. and Abrahams, J. P. (2019) “Reducing dynamical electron scattering reveals hydrogen atoms”, Acta crystallographica. Section A, Foundations and advances, 75(Pt 1), pp. 82–93. doi: 10.1107/S2053273318013918.   edoc
Moradi, M., Opara, N. L., Tulli, L. G., Wäckerlin, C., Dalgarno, S. J., Teat, S. J., Baljozovic, M., Popova, O., van Genderen, E., Kleibert, A., Stahlberg, H., Abrahams, J. P., Padeste, C., Corvini, P. F.-X., Jung, T. A. and Shahgaldian, P. (2019) “Supramolecular architectures of molecularly thin yet robust free-standing layers”, Science Advances. American Association for the Advancement of Science, 5(2), p. eaav4489. doi: 10.1126/sciadv.aav4489.   edoc
Merg, A. D., van Genderen, E., Bazrafshan, A., Su, H., Zuo, X., Touponse, G., Blum, T. B., Salaita, K., Abrahams, J. P. and Conticello, V. P. (2019) “Seeded Heteroepitaxial Growth of Crystallizable Collagen Triple Helices: Engineering Multifunctional Two-Dimensional Core-Shell Nanostructures”, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. AMER CHEMICAL SOC, 141(51), pp. 20107–20117. doi: 10.1021/jacs.9b09335.   edoc
Blum, T. B., Filippidou, S., Fatton, M., Junier, P. and Abrahams, J. P. (2019) “The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo”, Scientific reports, 9(1), p. 14948. doi: 10.1038/s41598-019-51440-1.   edoc
Latychevskaia, T. and Abrahams, J. P. (2019) “Inelastic scattering and solvent scattering reduce dynamical diffraction in biological crystals”, Acta Crystallographica Section B-Structural Science Crystal Engineering and Materials. International Union of Crystallography, 75, pp. 523–531. doi: 10.1107/S2052520619009661.   edoc
Clabbers, M., Gruene, T., van Genderen, E. and Abrahams, J. P. (2018) “Experimental and computational reduction of dynamical electron scattering allows visualizing individual hydrogen atoms”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S2053273318088770.   edoc
Abrahams, J. P., Clabbers, M., van Genderen, E. and Blum, T. (2018) “Electron tomography of radiation sensitive 3D nano-crystals in imaging and diffraction mode”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S205327331809397X.   edoc
Tinti, G., Fröjdh, E., van Genderen, E., Gruene, T., Schmitt, B., de Winter, D. A. M., Weckhuysen, B. M. and Abrahams, J. P. (2018) “Electron crystallography with the EIGER detector”, IUCrJ, 5(Pt 2), pp. 190–199. doi: 10.1107/S2052252518000945.   edoc
Wallin, C., Hiruma, Y., Wärmländer, S. K. T. S., Huvent, I., Jarvet, J., Abrahams, J. P., Gräslund, A., Lippens, G. and Luo, J. (2018) “The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage”, Journal of the American Chemical Society, pp. 8138–8146. doi: 10.1021/jacs.7b13623.   edoc
Thomas, B., Dubey, R. K., Clabbers, M. T. B., Gupta, K. B. S. S., van Genderen, E., Jager, W. F., Abrahams, J. P., Sudholter, E. J. R. and de Groot, H. J. M. (2018) “A Molecular Level Approach To Elucidate the Supramolecular Packing of Light-Harvesting Antenna Systems”, Chemistry (Weinheim an der Bergstrasse, Germany), 24(56), pp. 14989–14993. doi: 10.1002/chem.201802288.   edoc
Clabbers, M. T. B., Gruene, T., Parkhurst, J. M., Abrahams, J. P. and Waterman, D. G. (2018) “Electron diffraction data processing with DIALS”, Acta crystallographica. Section D, Structural biology, 74(Pt 6), pp. 506–518. doi: 10.1107/S2059798318007726.   edoc
Clabbers, M. T. B. and Abrahams, J. P. (2018) “Electron diffraction and three-dimensional crystallography for structural biology”, CRYSTALLOGRAPHY REVIEWS. TAYLOR & FRANCIS LTD, 24(3), pp. 176–204. doi: 10.1080/0889311X.2018.1446427.   edoc
Tinti, G., Frojdh, E., Van Genderen, E., Gruene, T., Schmitt, B., De Winter, D. A. M., Weckhuysen, B. M. and Abrahams, J. P. (2018) “CCDC 1817054: Experimental Crystal Structure Determination”, Cambridge Structural Database, p. 1817054. doi: 10.5517/ccdc.csd.cc1yzsnc.   edoc
Matheson, J., Moldovan, G., Kirkland, A., Allinson, N. and Abrahams, J. P. (2017) “Testing and Comparison of Imaging Detectors for Electrons in the Energy Range 10–20 keV”, Journal of Instrumentation. IOP Publishing, 12(11), p. C11016. doi: 10.1088/1748-0221/12/11/C11016.   edoc
Nederlof, I., van Genderen, E., Clabbers, M. E. and Abrahams, J. P. (2017) “Electron Crystallography of Protein Nano-Crystals ”, Acta Crystallographica Section A: Foundations And Advances. International Union of Crystallography, A73, pp. a297-a298.   edoc
Nikolopoulos, S., Galanis, A. S., Vallcorba, O., Eggeman, A., Das, P. P., Abrahams, J. P., Rauch, E., Midgley, P. and Gemmi, M. (2017) “Random electron diffraction tomography for structure analysis of pharmaceuticals ”, Acta Crystallographica A-Foundation And Advances. Edited by International Union of Crystallography. Wiley, 73, p. c980. Available at: https://journals.iucr.org/a/issues/2017/a2/00/a56076/a56076.pdf.   edoc
Yin, Q., Liu, Z., Laroche, F., Zhou, X., Shao, N., Lin, B., Wang, R., Yuan, N., Ding, J. and Abrahams, J. P. (2017) “A Novel Capturing Method for Quantification of Extra-Cellular Nanovesicles ”, Journal of nanoscience and nanotechnology. American Scientific, 17(2), pp. 908–913. doi: 10.1166/jnn.2017.12631.   edoc
Clabbers, M. T. B., van Genderen, E., Wan, W., Wiegers, E. L., Gruene, T. and Abrahams, J. P. (2017) “Protein structure determination by electron diffraction using a single three-dimensional nanocrystal”, Acta crystallographica. Section D, Structural biology, 73(Pt 9), pp. 738–748. doi: 10.1107/S2059798317010348.   edoc
Su, J., Wang, H., Wu, K., Liu, Z., Yin, Q., Wang, R., Lv, W., Yin, S., Liu, Z. and Abrahams, J. P. (2017) “Neutravidin-Mediated Extraction of Isolated Small Diameter Single Walled Carbon Nanotubes for Bio-Recognition”, Journal of nanoscience and nanotechnology, 17(5), pp. 3588–3596. doi: 10.1166/jnn.2017.12860.   edoc
Wang, R., Boleij, M., Yin, Q., Galjart, N., Lin, B., Yuan, N., Zhou, X., Tan, M., Ding, J., Liu, Z. and Abrahams, J. P. (2017) “Purification of Biotinylated Proteins Using Single Walled Carbon Nanotube-Streptavidin Complexes”, Journal of nanoscience and nanotechnology, 17(2), pp. 926–931. doi: 10.1166/jnn.2017.12716.   edoc
Abrahams, J. P. (2016) “Electron nanodiffraction for structural biology”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography, 72(a1), p. s6. doi: 10.1107/S2053273316099903.   edoc
Wallin, C., Kulkarni, Y. S., Abelein, A., Jarvet, J., Liao, Q., Strodel, B., Olsson, L., Luo, J., Abrahams, J. P., Sholts, S. B., Roos, P. M., Kamerlin, S. C. L., Gräslund, A. and Wärmländer, S. K. T. S. (2016) “Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer’s disease”, Journal of Trace Elements in Medicine and Biology. Urban & Fischer, 38, pp. 183–193. doi: 10.1016/j.jtemb.2016.03.009.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. and Abrahams, J. P. (2016) “Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II”, ACS Chemical Neuroscience . American Chemical Society, 7(3), pp. 269–274. doi: 10.1021/acschemneuro.5b00325.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. and Abrahams, J. P. (2016) “Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis”, Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 291(32), pp. 16485–16493. doi: 10.1074/jbc.R116.714576.   edoc
van Genderen, E., Clabbers, M. T. B., Das, P. P., Stewart, A., Nederlof, I., Barentsen, K. C., Portillo, Q., Pannu, N. S., Nicolopoulos, S., Gruene, T. and Abrahams, J. P. (2016) “Ab initio structure determination of nanocrystals of organic pharmaceutical compounds by electron diffraction at room temperature using a Timepix quantum area direct electron detector”, Acta Crystallographica Section A : Foundations and Advances. International Union of Crystallography, 72(2), pp. 236–242. doi: 10.1107/S2053273315022500.   edoc
Tiiman, A., Luo, J., Wallin, C., Olsson, L., Lindgren, J., Jarvet, J., Per, R., Sholts, S. B., Rahimipour, S., Abrahams, J. P., Karlström, A. E., Gräslund, A. and Wärmländer, S. K. T. S. (2016) “Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species”, Journal of Alzheimer’s Disease. IOS Press, 54(3), pp. 971–982. doi: 10.3233/JAD-160427.   edoc
Afanasyev, P., Ravelli, R. B. G., Matadeen, R., De Carlo, S., van Duinen, G., Alewijnse, B., Peters, P. J., Abrahams, J.-P., Portugal, R. V., Schatz, M. and van Heel, M. (2015) “A posteriori correction of camera characteristics from large image data sets”, Scientific Reports. Nature Publishing Group, 5, p. 10317. doi: 10.1038/srep10317.   edoc
Clabbers, M. T. B., van Genderen, E., Nederlof, I., Li, Y.-W. and Abrahams, J. P. (2015) “Electron crystallography of 3D nano-crystals”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S2053273315093985.   edoc
Abrahams, J. P., van Genderent, E., Nederlof, I., Clabbers, M. and Li, Y. (2015) “Electron diffraction and imaging of 3D nanocrystals of pharmaceuticals, peptides and proteins”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S2053273315098496.   edoc
Luo, J. and Abrahams, J. P. (2014) “Cyclic Peptides as Inhibitors of Amyloid Fibrillation ”, Chemistry - A European Journal. Wiley, 20(9), pp. 2410–2419. doi: 10.1002/chem.201304253.   edoc
Luo, J., Wärmländer, S. K. T. S., Chien-Hung, Y., Muhammad, K., Gräslund, A. and Abrahams, J. P. (2014) “The Aβ peptide forms non-amyloid fibrils in the presence of carbon nanotubes”, Nanoscale. Royal Society of Chemistry, 6(12), pp. 6720–6726. doi: 10.1039/c4nr00291a.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. and Abrahams, J. P. (2014) “Alzheimer Peptides Aggregate into Transient Nanoglobules That Nucleate Fibrils”, Biochemistry. American Chemical Society, 53(40), pp. 6302–6308. doi: 10.1021/bi5003579.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. and Abrahams, J. P. (2014) “Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid beta Peptide”, Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 289(40), pp. 27766–27775. doi: 10.1074/jbc.M114.574947.   edoc
Abelein, A., Abrahams, J. P., Danielsson, J., Graslund, A., Jarvet, J., Luo, J., Tiiman, A. and Warmlander, S. K. T. S. (2014) “The hairpin conformation of the amyloid beta peptide is an important structural motif along the aggregation pathway ”, Journal of Biological Inorganic Chemistry. Springer, 19(4-5), pp. 623–634. doi: 10.1007/s00775-014-1131-8.   edoc
Luo, J., Mohammed, I., Warmlander, S. K. T. S., Hiruma, Y., Graslund, A. and Abrahams, J. P. (2014) “Endogenous Polyamines Reduce the Toxicity of Soluble A beta Peptide Aggregates Associated with Alzheimer’s Disease”, Biomacromolecules. American Chemical Societ, 15(6), pp. 1985–1991. doi: 10.1021/bm401874j.   edoc
Liu, Z., Voskamp, P., Zhang, Y., Chu, F. and Abrahams, J. P. (2013) “Capture of unstable protein complex on the streptavidin-coated single-walled carbon nanotubes ”, Journal of Nanoparticle Research. Springer, 15(4), p. A 1582. doi: 10.1007/s11051-013-1582-9.   edoc
Luo, J., Yu, C.-H., Yu, H., Borstnar, R., Kamerlin, S. C. L., Gräslund, A., Abrahams, J. P. and Wärmländer, S. K. T. S. (2013) “Cellular Polyamines Promote Amyloid-Beta Peptide Fibrillation and Modulate the Aggregation Pathways”, Biophysical Journal. Cell Press. doi: 10.1016/j.bpj.2012.11.2170.   edoc
Nederlof, I., Li, Y. W., van Heel, M. and Abrahams, J. P. (2013) “Imaging protein three-dimensional nanocrystals with cryo-EM”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 69, pp. 852–859. doi: 10.1107/S0907444913002734.   edoc
Luo, J., Yu, C.-H., Yu, H., Borstnar, R., Kamerlin, S. C. L., Gräslund, A., Abrahams, J. P. and Wärmländer, S. K. T. S. (2013) “Cellular Polyamines Promote Amyloid-Beta (A beta) Peptide Fibrillation and Modulate the Aggregation Pathways”, ACS Chemical Neuroscience . American Chemical Society, 4(3), pp. 454–462. doi: 10.1021/cn300170x.   edoc
Nederlof, I., van Genderen, E., Li, Y.-W. and Abrahams, J. P. (2013) “A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 69, pp. 1223–1230. doi: 10.1107/S0907444913009700.   edoc
Luo, J., Zwier, R. and Abrahams, J. P. (2013) “An efficient nanolitre-volume multi-channel device for highly viscous materials used in membrane protein crystallization”, Journal of applied crystallography. Wiley-Blackwell, 46, pp. 829–831. doi: 10.1107/S0021889813006742.   edoc
Luo, J., Wärmländer, S. K. T. S., Gräslund, A. and Abrahams, J. P. (2013) “Human lysozyme inhibits the in vitro aggregation of Aβ peptides, which in vivo are associated with Alzheimer’s disease”, Chemical Communications . Royal Society of Chemistry, 49(58), pp. 6507–6509. doi: 10.1039/c3cc42325e.   edoc
Luo, J., Otero, J. M., Yu, C.-H., Wärmländer, S. K. T. S., Gräslund, A., Overhand, M. and Abrahams, J. P. (2013) “Inhibiting and Reversing Amyloid‐β Peptide (1–40) Fibril Formation with Gramicidin S and Engineered Analogues ”, Chemistry - A European Journal. Wiley, 19(51), pp. 17338–17348. doi: 10.1002/chem.201301535.   edoc
ten Bruggencate, F., Laroche, F., Zhang, Y., Song, G., Yin, S., Abrahams, J. P. and Liu, Z. (2013) “Visualizing the localization of transfection complexes during graphene nanoparticle-based transfection”, Journal of Materials Chemistry B. Royal Society of Chemistry, 1(46), pp. 6353–6358. doi: 10.1039/c3tb21349h.   edoc
Meulenbroek, E. M., Thomassen, E. A. J., Pouvreau, L., Abrahams, J. P., Gruppen, H. and Pannu, N. S. (2012) “Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 68(Pt 7), pp. 794–799. doi: 10.1107/S090744491201222X.   edoc
Liu, Z., Galli, F., Waterreus, W.-J., Meulenbroek, E., Koning, R. I., Lamers, G. E. M., Olsthoorn, R. C. L., Pannu, N., Oosterkamp, T. H., Koster, A. J., Dame, R. T. and Abrahams, J. P. (2012) “Single-walled carbon nanotubes as scaffolds to concentrate DNA for the study of DNA-protein interactions”, ChemPhysChem. Wiley, 13(6), pp. 1569–1575. doi: 10.1002/cphc.201100896.   edoc
Nederlof, I., Georgieva, D. and Abrahams, J. P. (2011) “Electron diffraction of submicron 3D protein crystals”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S010876731109430X.   edoc
Nicolopoulos, S., Rauch, E., Georgieva, D. and Abrahams, J. P. (2011) “Low resolution electron crystallography challenges in organic and inorganic crystals with transmission electron microscope (TEM)”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S0108767311095304.   edoc
Waterreus, W.-J., Skubák, P., Sikharulidze, I., Abrahams, J. P., de Graaff, R. A. G. and Pannu, N. S. (2011) “Advances in the CRANK software suite for automated crystal structure solution”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S0108767311083346.   edoc
Abrahams, J.-P., Apweiler, R., Balling, R., Bertero, M. G., Bujnicki, J. M., Chayen, N. E., Chène, P., Corthals, G. L., Dyląg, T., Förster, F., Heck, A. J. R., Henderson, P. J. F., Herwig, R., Jehenson, P., Kokalj, S. J., Laue, E., Legrain, P., Martens, L., Migliorini, C., Musacchio, A., Podobnik, M., Schertler, G. F. X., Schreiber, G., Sixma, T. K., Smit, A. B., Stuart, D., Svergun, D. I. and Taussig, M. J. (2011) “‘4D Biology for health and disease’ workshop report”, New biotechnology. Elsevier, 28(4), pp. 291–293. doi: 10.1016/j.nbt.2010.10.003.   edoc
Jiang, L., Georgieva, D., Nederlof, I., Liu, Z. and Abrahams, J. P. (2011) “Image processing and lattice determination for three-dimensional nanocrystals”, Microscopy and Microanalysis. Cambridge University Press, 17(6), pp. 879–885. doi: 10.1017/S1431927611012244.   edoc
Pannu, N. S., Waterreus, W. J., Skubák, P., Sikharulidze, I., Abrahams, J. P. and de Graaff, R. A. G. (2011) “Recent advances in the CRANK software suite for experimental phasing”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 67(Pt 4), pp. 331–337. doi: 10.1107/S0907444910052224.   edoc
Sikharulidze, I., Van Gastel, R., Schramm, S., Abrahams, J. P., Poelsema, B., Trom, R. M. and Van der Molen, S. J. (2010) “Improved Imaging in low Energy Electron Microscopy and Photo Emission Electron Microscopy Using Medipix2 Pixel Detector”, in Leroy, C., Rancoita, P.-G., Barone, M., Gaddi, A., Price, L., and Ruchti, R. (eds.) Astroparticle, Particle and Space Physics, Detectors and Medical Physics Applications. Proceedings of the 11th Conference, Villa Olmo, Como, Italy, 5-9 October 2009. Singapore: World Scientific (Astroparticle, Particle, Space Physics, Radiation Interaction, Detectors and Medical Physics Applications), pp. 133–139. doi: 10.1142/9789814307529_0023.   edoc
Abrahams, J. P. (2010) “The strong phase object approximation may allow extending crystallographic phases of dynamical electron diffraction patterns of 3D protein nano-crystals”, Zeitschrift für Kristallographie - Crystalline Materials. De Gruyter Oldenbourg, 225(2-3), pp. 67–76. doi: 10.1524/zkri.2010.1216.   edoc
Liu, Z., Galli, F., Janssen, K. G. H., Jiang, L., van der Linden, H. J., de Geus, D. C., Voskamp, P., Kuil, M. E., Olsthoorn, R. C. L., Oosterkamp, T. H., Hankemeier, T. and Abrahams, J. P. (2010) “Stable Single-Walled Carbon Nanotube-Streptavidin Complex for Biorecognition”, Journal of Physical Chemistry C. American Chemical Society, 114(10), pp. 4345–4352. doi: 10.1021/jp911441d.   edoc
Liu, Z., Jiang, L., Galli, F., Nederlof, I., Olsthoorn, R. C. L., Lamers, G. E. M., Oosterkamp, T. H. and Abrahams, J. P. (2010) “A Graphene Oxide center dot Streptavidin Complex for Biorecognition - Towards Affinity Purification”, Advanced Functional Materials. Wiley, 20(17), pp. 2857–2865. doi: 10.1002/adfm.201000761; 10.1002/adfm.201000761.   edoc
Jiang, L., Liu, Z., Georgieva, D., Kuil, M. E. and Abrahams, J. P. (2010) “A novel approximation method of CTF amplitude correction for 3D single particle reconstruction”, Ultramicroscopy. Elsevier, 110(4), pp. 350–358. doi: 10.1016/j.ultramic.2010.01.011.   edoc
Jiang, L., Georgieva, D., IJspeert, K. and Abrahams, J. P. (2009) “An intelligent peak search program for digital electron diffraction images of 3D nano-crystals”, in Qiu, P., Yiu, C., Zhang, H., and Wen, X. (eds.) 2009 2nd International Congress on Image and Signal Processing. IEEE, pp. 1–5. doi: 10.1109/CISP.2009.5301421.   edoc
Abrahams, J. P., Jiang, L., Sikhuralidze, I., Nederloff, I., Zandbergen, H. and Georgieva, D. (2009) “Macromolecular Electron Crystallography”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S0108767309099875.   edoc
Waterreus, W.-J., Pannu, N., Skubák, P., Sikharulidze, I., Abrahams, J. P. and de Graaff, R. A. G. (2009) “Recent Advances in CRANK”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S0108767309096743.   edoc
de Geus, D. C., Thomassen, E. A. J., Hagedoorn, P.-L., Pannu, N. S., van Duijn, E. and Abrahams, J. P. (2009) “Crystal Structure of Chlorite Dismutase, a Detoxifying Enzyme Producing Molecular Oxygen”, Journal of Molecular Biology. Elsevier, 387(1), pp. 192–206. doi: 10.1016/j.jmb.2009.01.036.   edoc
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., Abrahams, J. P., Goosen, N. and Pannu, N. S. (2009) “Involvement of a carboxylated lysine in UV damage endonuclease”, Protein Science. Wiley, 18(3), pp. 549–558. doi: 10.1002/pro.54.   edoc
Jiang, L., Schaffitzel, C., Bingel-Erlenmeyer, R., Ban, N., Korber, P., Koning, R. I., de Geus, D. C., Plaisier, J. R. and Abrahams, J. P. (2009) “Recycling of Aborted Ribosomal 50S Subunit-Nascent Chain-tRNA Complexes by the Heat Shock Protein Hsp15”, Journal of Molecular Biology. Elsevier, 386(5), pp. 1357–1367. doi: 10.1016/j.jmb.2008.10.079.   edoc
Jiang, L., Georgieva, D., Zandbergen, H. W. and Abrahams, J. P. (2009) “Unit-cell determination from randomly oriented electron-diffraction patterns”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 65, pp. 625–632. doi: 10.1107/S0907444909003163.   edoc
Pannu, N. S., Ravelli, R. B. G. and Abrahams, P. (2009) “The Max-Inf2/Lorentz Center workshop on New algorithms in macromolecular crystallography and electron microscopy”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 65, pp. 623–624. doi: 10.1107/S0907444909020861.   edoc
van Gastel, R., Sikharulidze, I., Schramm, S., Abrahams, J. P., Poelsema, B., Tromp, R. M. and van der Molen, S. J. (2009) “Medipix 2 detector applied to low energy electron microscopy”, Ultramicroscopy. Elsevier, 110(1), pp. 33–35. doi: 10.1016/j.ultramic.2009.09.002.   edoc
van Haren, J., Draegestein, K., Keijzer, N., Abrahams, J. P., Grosveld, F., Peeters, P. J., Moechars, D. and Galjart, N. (2009) “Mammalian Navigators are Microtubule Plus-End Tracking Proteins that can Reorganize the Cytoskeleton to Induce Neurite-Like Extensions”, Cell Motility and the Cytoskeleton . Wiley, 66(10), pp. 824–838. doi: 10.1002/cm.20370.   edoc
de Geus, D. C., van Roon, A.-M. M., Thomassen, E. A. J., Hokke, C. H., Deelder, A. M. and Abrahams, J. P. (2009) “Characterization of a diagnostic Fab fragment binding trimeric Lewis X”, Proteins: Structure, Function, and Bioinformatics . Wiley-Blackwell, 76(2), pp. 439–447. doi: 10.1002/prot.22356.   edoc
De Geus, D. C., Van Roon, A. M. M., Thomassen, E. A. J., Hokke, C. H., Deelder, A. M. and Abrahams, J. P. (2009) “2VQ1: Anti Trimeric Lewis X Fab54-5C10-A”, Worldwide Protein Data Bank, p. 2VQ1. doi: 10.2210/pdb2vq1/pdb.   
De Geus, D. C., Thomassen, E. A. J., Hagedoorn, P. L., Pannu, N. S. and Abrahams, J. P. (2009) “2VXH: The Crystal Structure Of Chlorite Dismutase: A Detox Enzyme Producing Molecular Oxygen”, Worldwide Protein Data Bank, p. 2VXH. doi: 10.2210/pdb2vxh/pdb.   
Abrahams, J. P., Georgieva, D., Jiang, L. and Zandbergen, H. W. (2008) “Prospects for structure solution by electron diffraction of three-dimensional protein crystals”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S0108767308097584.   edoc
Zovko, S., Abrahams, J. P., Koster, A. J., Galjart, N. and Mommaas, A. M. (2008) “Microtubule plus-end conformations and dynamics in the periphery of interphase mouse fibroblasts”, Molecular Biology of the Cell. American Society for Cell Biology, 19(7), pp. 3138–3146. doi: 10.1091/mbc.E07-07-0681.   edoc
de Geus, D. C., Thomassen, E. A. J., van der Feltz, C. L. and Abrahams, J. P. (2008) “Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of chlorite dismutase: a detoxifying enzyme producing molecular oxygen”, Acta Crystallographica Section F. Wiley, 64, pp. 730–732. doi: 10.1107/S1744309108020551.   edoc
Jiang, L., Schaffitzel, C., Bingel-Erlenmeyer, R., Ban, N., Korber, P., Koning, R. I., Plaisier, J. R. and Abrahams, J. P. (2008) “EMD-1455: Recycling of Aborted Ribosomal 50S Subunit-Nascent Chain-tRNA Complexes by the Heat Shock Protein Hsp15”, Electron Microscopy Data Bank, p. EMD–1455.   
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., Abrahams, J. P., Goosen, N. and Pannu, N. S. (2008) “3C0S: UVDE 3 metals”, Worldwide Protein Data Bank, p. 3C0S. doi: 10.2210/pdb3c0s/pdb.   
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., Abrahams, J. P., Goosen, N. and Pannu, N. S. (2008) “3C0Q: Uvde E175a”, Worldwide Protein Data Bank, p. 3C0Q. doi: 10.2210/pdb3c0q/pdb.   
Jiang, L. and Abrahams, J. P. (2008) “3BBX: The Hsp15 protein fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex”, Worldwide Protein Data Bank, p. 3BBX. doi: 10.2210/pdb3bbx/pdb.   
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., Abrahams, J. P., Goosen, N. and Pannu, N. S. (2008) “3C0L: Uvde K229r”, Worldwide Protein Data Bank, p. 3C0L. doi: 10.2210/pdb3c0l/pdb.   
Jiang, L. and Abrahams, J. P. (2008) “3BBU: The Hsp15 protein fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex”, Worldwide Protein Data Bank, p. 3BBU. doi: 10.2210/pdb3bbu/pdb.   
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., Abrahams, J. P., Goosen, N. and Pannu, N. S. (2008) “3BZJ: Uvde K229l”, Worldwide Protein Data Bank, p. 3BZJ. doi: 10.2210/pdb3bzj/pdb.   
Jiang, L. and Abrahams, J. P. (2008) “3BBV: The tRNA(phe) fitted into the low resolution Cryo-EM map of the 50S.nc-tRNA.Hsp15 complex”, Worldwide Protein Data Bank, p. 3BBV. doi: 10.2210/pdb3bbv/pdb.   
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. and Ban, N. (2008) “EMD-1250.map”, Electron Microscopy Data Bank, p. EMD–1250.map.   
Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., Abrahams, J. P., Goosen, N. and Pannu, N. S. (2008) “3BZG: UVDE pH4.4”, Worldwide Protein Data Bank, p. 3BZG. doi: 10.2210/pdb3bzg/pdb.   
Jiang, L., Schaffitzel, C., Bingel-Erlenmeyer, R., Ban, N., Korber, P., Koning, R. I., Plaisier, J. R. and Abrahams, J. P. (2008) “EMD-1456.map”, Electron Microscopy Data Bank, p. EMD–1456.map.   
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. and Ban, N. (2008) “EMD-1251: Structure of the E. coli signal recognition particle bound to a translating ribosome”, Electron Microscopy Data Bank, p. EMD–1251.   
Paspaleva, K., Thomassen, E., Pannu, N. S., Iwai, S., Moolenaar, G. F., Goosen, N. and Abrahams, J. P. (2007) “Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease”, Structure. Cell Press, 15(10), pp. 1316–1324. doi: 10.1016/j.str.2007.05.010.   edoc
Georgieva, D. G., Kuil, M. E., Oosterkamp, T. H., Zandbergen, H. W. and Abrahams, J. P. (2007) “Heterogeneous nucleation of three-dimensional protein nanocrystals”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 63, pp. 564–570. doi: 10.1107/S0907444907007810.   edoc
Plaisier, J. R., Jiang, L. and Abrahams, J. P. (2007) “Cyclops: New modular software suite for cryo-EM”, Journal of structural biology. Academic Press, 157(1), pp. 19–27. doi: 10.1016/j.jsb.2006.07.002.   edoc
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. and Ban, N. (2007) “Erratum: Structure of the E-coli signal recognition particle bound to a translating ribosome (vol 444, pg 503, 2006)”, Nature. Macmillan, 448(7157), p. 1076. doi: 10.1038/nature06169.   edoc
Thomassen, E. A. J., Dekking, E. H. A., Thompson, A., Franken, K. L., Sanal, Ö., Abrahams, J. P., van Tol, M. J. D. and Koning, F. (2006) “The Impact of Single Amino Acid Substitutions in CD3γ on the CD3ϵγ Interaction and T-Cell Receptor–CD3 Complex Formation”, Human immunology. Elsevier, 67(8), pp. 579–588. doi: 10.1016/j.humimm.2006.04.015.   edoc
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. and Ban, N. (2006) “Structure of the E. coli signal recognition particle bound to a translating ribosome”, Nature. Nature Research, 444(7118), pp. 503–506. doi: 10.1038/nature05182.   edoc
Kuil, M. E., Abrahams, J. P. and Marijnissen, J. C. M. (2006) “Nano-dispensing by electrospray for biotechnology”, Biotechnology journal. Wiley, 1(9), pp. 969–975. doi: 10.1002/biot.200600062.   edoc
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. and Ban, N. (2006) “STRUCTURE OF THE E. COLI SIGNAL RECOGNITION PARTICLE BOUND TO A TRANSLATING RIBOSOME”, Nucleic Acid Database, p. 2iy3. doi: 10.2210/pdb2iy3/pdb.   
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I. and Ban, N. (2006) “2IY3: Structure of the E. Coli Signal Regognition Particle”, Worldwide Protein Data Bank, p. 2IY3. doi: 10.2210/pdb2iy3/pdb.   
Schmauder, R., van Rijn, R., Abrahams, J. P., Kuil, M. E. and Schmidt, T. (2005) “FCS in non-ideal solutions”, Biophysical Journal. Biophysical Society.   edoc
Thomassen, E. A. J., van Veen, H. A., van Berkel, P. H. C., Nuijens, J. H. and Abrahams, J. P. (2005) “The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin”, Transgenic Research. Springer, 14(4), pp. 397–405. doi: 10.1007/s11248-005-3233-0.   edoc
Ness, S. R., de Graaff, R. A. G., Abrahams, J. P. and Pannu, N. S. (2004) “CRANK - New Methods for Automated Structure Solution”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S0108767304099702.   edoc
Leliveld, S. R., Dame, R. T., Rohn, J. L., Noteborn, M. H. M. and Abrahams, J. P. (2004) “Apoptin’s functional N- and C-termini independently bind DNA”, FEBS Letters. Elsevier, 557(1-3), pp. 155–158. doi: 10.1016/S0014-5793(03)01465-0.   edoc
Thomassen, E. A. J., Pouvreau, L., Gruppen, H. and Abrahams, J. P. (2004) “Crystallization and preliminary X-ray crystallographic studies on a Kunitz-type potato serine protease inhibitor”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 60(Pt 8), pp. 1464–1466. doi: 10.1107/S0907444904013484.   edoc
van Roon, A.-M. M., Bink, H. H. J., Plaisier, J. R., Pleij, C. W. A., Abrahams, J. P. and Pannu, N. S. (2004) “Crystal structure of an empty capsid of turnip yellow mosaic virus”, Journal of Molecular Biology. Elsevier, 341(5), pp. 1205–1214. doi: 10.1016/j.jmb.2004.06.085.   edoc
Ness, S. R., de Graaff, R. A. G., Abrahams, J. P. and Pannu, N. S. (2004) “CRANK: new methods for automated macromolecular crystal structure solution”, Structure. Cell Press, 12(10), pp. 1753–1761. doi: 10.1016/j.str.2004.07.018.   edoc
Plaisier, J. R., Koning, R. I., Koerten, H. K., van Heel, M. and Abrahams, J. P. (2004) “TYSON: robust searching, sorting, and selecting of single particles in electron micrographs”, Journal of Structural Biology. Elsevier, 145(1-2), pp. 76–83. doi: 10.1016/j.jsb.2003.09.030.   edoc
van Roon, A.-M. M., Pannu, N. S., de Vrind, J. P. M., van der Marel, G. A., van Boom, J. H., Hokke, C. H., Deelder, A. M. and Abrahams, J. P. (2004) “Structure of an anti-Lewis X Fab fragment in complex with its Lewis X antigen”, Structure. Cell Press, 12(7), pp. 1227–1236. doi: 10.1016/j.str.2004.05.008.   edoc
Bos, I. G. A., Lubbers, Y. T. P., Eldering, E., Abrahams, J. P. and Hack, C. E. (2004) “Effect of reactive site loop elongation on the inhibitory activity of C1-inhibitor”, Biochimica et Biophysica Acta - Proteins and Proteomics. Elsevier, 1699(1-2), pp. 139–144. doi: 10.1016/j.bbapap.2004.02.006.   edoc
Van Roon, A. M. M., Pannu, N. S., De Vrind, J. P. M., Hokke, C. H., Deelder, A. M., Van Der Marel, G. A., Van Boom, J. H. and Abrahams, J. P. (2004) “1UZ8: Anti-Lewis X Fab Fragment In Complex With Lewis X”, Worldwide Protein Data Bank, p. 1UZ8. doi: 10.2210/pdb1uz8/pdb.   
Van Roon, A. M. M., Bink, H. H. J., Plaisier, J. R., Pleij, C. W. A., Abrahams, J. P. and Pannu, N. S. (2004) “1W39: Crystal Structure Of An Artificial Top Component Of Turnip Yellow Mosaic Virus”, Worldwide Protein Data Bank, p. 1W39. doi: 10.2210/pdb1w39/pdb.   
Van Roon, A. M. M., Pannu, N. S., De Vrind, J. P. M., Hokke, C. H., Deelder, A. M., Van Der Marel, G. A., Van Boom, J. H. and Abrahams, J. P. (2004) “1UZ6: Anti-Lewis X Fab Fragment Uncomplexed”, Worldwide Protein Data Bank, p. 1UZ6. doi: 10.2210/pdb1uz6/pdb.   
Schmauder, R., Schmidt, T., Abrahams, J. P. and Kuil, M. E. (2003) “Screening Crystallisation conditions using Fluorescence Correlation Spectroscopy”, Biophysical Journal. Biophysical Society.   edoc
Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. and Abrahams, J. P. (2003) “ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase”, Nature Structural Biology. Nature Publishing Group, 10(6), pp. 468–474. doi: 10.1038/nsb924.   edoc
Zhang, Y.-H., Leliveld, S. R., Kooistra, K., Molenaar, C., Rohn, J. L., Tanke, H. J., Abrahams, J. P. and Noteborn, M. H. M. (2003) “Recombinant Apoptin multimers kill tumor cells but are nontoxic and epitope-shielded in a normal-cell-specific fashion”, Experimental Cell Research. Elsevier, 289(1), pp. 36–46. doi: 10.1016/S0014-4827(03)00188-5.   edoc
Abrahams, J. P. and Thomassen, E. A. J. (2003) “Mechanism of thrombin’s enigmatic sodium switch revealed”, Structure. Cell Press, 11(4), pp. 363–364. doi: 10.1016/S0969-2126(03)00056-X.   edoc
Danen-van Oorschot, A. A. A. M., Zhang, Y.-H., Leliveld, S. R., Rohn, J. L., Seelen, M. C. M. J., Bolk, M. W., van Zon, A., Erkeland, S. J., Abrahams, J.-P., Mumberg, D. and Noteborn, M. H. M. (2003) “Importance of nuclear localization of apoptin for tumor-specific induction of apoptosis”, Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 278(30), pp. 27729–27736. doi: 10.1074/jbc.M303114200.   edoc
Bos, I. G. A., Lubbers, Y. T. P., Roem, D., Abrahams, J. P., Hack, C. E. and Eldering, E. (2003) “The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant”, Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 278(32), pp. 29463–29470. doi: 10.1074/jbc.M302977200.   edoc
Leliveld, S. R., Dame, R. T., Mommaas, M. A., Koerten, H. K., Wyman, C., Danen-van Oorschot, A. A. A. M., Rohn, J. L., Noteborn, M. H. M. and Abrahams, J. P. (2003) “Apoptin protein multimers form distinct higher-order nucleoprotein complexes with DNA”, Nucleic Acids Research. Oxford University Press, 31(16), pp. 4805–4813. doi: 10.1093/nar/gkg661.   edoc
Thomassen, E., Gielen, G., Schutz, M., Schoehn, G., Abrahams, J. P., Miller, S. and van Raaij, M. J. (2003) “The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold”, Journal of Molecular Biology. Elsevier, 331(2), pp. 361–373. doi: 10.1016/S0022-2836(03)00755-1.   edoc
Leliveld, S. R., Noteborn, M. H. M. and Abrahams, J. P. (2003) “Prevalent conformations and subunit exchange in the biologically active apoptin protein multimer”, European Journal of Biochemistry. Wiley, 270(17), pp. 3619–3627. doi: 10.1046/j.1432-1033.2003.03750.x.   edoc
Koning, R., van den Worm, S., Plaisier, J. R., van Duin, J., Abrahams, J. P. and Koerten, H. (2003) “Visualization by cryo-electron microscopy of genomic RNA that binds to the protein capsid inside bacteriophage MS2”, Journal of Molecular Biology. Elsevier, 332(2), pp. 415–422. doi: 10.1016/S0022-2836(03)00846-5.   edoc
Plaisier, J. R., Koning, R. I., Koerten, H. K., van Roon, A. M., Thomassen, E. A. J., Kuil, M. E., Hendrix, J., Broennimann, C., Pannu, N. S. and Abrahams, J. P. (2003) “Area detectors in structural biology”, Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment. Elsevier, 509(1-3), pp. 274–282. doi: 10.1016/S0168-9002(03)01638-3.   edoc
Leliveld, S. R., Zhang, Y.-H., Rohn, J. L., Noteborn, M. H. M. and Abrahams, J. P. (2003) “Apoptin induces tumor-specific apoptosis as a globular multimer”, Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 278(11), pp. 9042–9051. doi: 10.1074/jbc.M210803200.   edoc
McCoy, A. J., Pei, X. Y., Skinner, R., Abrahams, J.-P. and Carrell, R. W. (2003) “Structure of beta-antithrombin and the effect of glycosylation on antithrombin’s heparin affinity and activity”, Journal of Molecular Biology. Elsevier, 326(3), pp. 823–833. doi: 10.1016/S0022-2836(02)01382-7.   edoc
van Roon, A. M. M., Pannu, N. S., Hokke, C. H., Deelder, A. M. and Abrahams, J. P. (2003) “Crystallization and preliminary X-ray analysis of an anti-LewisX Fab fragment with and without its LewisX antigen”, Acta Crystallographica Section D. Wiley-Blackwell Publishing, 59, pp. 1306–1309. doi: 10.1107/S0907444903010096.   edoc
Hilge, M., Siegal, G., Vuister, G. W., Guentert, P., Gloor, S. M. and Abrahams, J. P. (2003) “1MO7: ATPase”, Worldwide Protein Data Bank, p. 1MO7. doi: 10.2210/pdb1mo7/pdb.   
Hilge, M., Siegal, G., Vuister, G. W., Guentert, P., Gloor, S. M. and Abrahams, J. P. (2003) “1MO8: ATPase”, Worldwide Protein Data Bank, p. 1MO8. doi: 10.2210/pdb1mo8/pdb.   
Hoedemaeker, F. J., Visschers, R. W., Alting, A. C., de Kruif, K. G., Kuil, M. E. and Abrahams, J. P. (2002) “A novel pH-dependent dimerization motif in beta-lactoglobulin from pig (Sus scrofa)”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 58, pp. 480–486. doi: 10.1107/S0907444902000616.   edoc
Kuil, M. E., Bodenstaff, E. R., Hoedemaeker, F. J. and Abrahams, J. P. (2002) “Protein nano-crystallogenesis”, Enzyme and Microbial Technology. Elsevier, 30(3), pp. 262–265. doi: 10.1016/S0141-0229(01)00496-3.   edoc
Bodenstaff, E. R., Hoedemaeker, F. J., Kuil, M. E., de Vrind, H. P. M. and Abrahams, J. P. (2002) “The prospects of protein nanocrystallography”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 58, pp. 1901–1906. doi: 10.1107/S0907444902016608.   edoc
Bos, I. G. A., Hack, C. E. and Abrahams, J. P. (2002) “Structural and functional aspects of C1-Inhibitor”, Immunobiology. Elsevier, 205(4-5), pp. 518–533. doi: 10.1078/0171-2985-00151.   edoc
Schmauder, R., Schmidt, T., Abrahams, J. P. and Kuil, M. E. (2002) “Screening crystallisation conditions using fluorescence correlation spectroscopy”, Acta Crystallographica Section D: Structural Biology. International Union of Crystallography, 58, pp. 1536–1541. doi: 10.1107/S0907444902014373.   edoc
Hilge, M., Perrakis, A., Abrahams, J. P., Winterhalter, K., Piontek, K. and Gloor, S. M. (2001) “Structure elucidation of beta-mannanase: from the electron-density map to the DNA sequence”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 57, pp. 37–43. doi: 10.1107/S0907444900015547.   edoc
de Graaff, R. A. G., Hilge, M., van der Plas, J. L. and Abrahams, J. P. (2001) “Matrix methods for solving protein substructures of chlorine and sulfur from anomalous data”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 57, pp. 1857–1862. doi: 10.1107/S0907444901016535.   edoc
McCoy, A. J., Skinner, R., Abrahams, J.-P., Pei, X. Y. and Carrell, R. W. (2000) “1E05: Plasma Alpha Antithrombin-Iii”, Worldwide Protein Data Bank, p. 100000. doi: 10.2210/pdb1e05/pdb.   
Abrahams, J. P. and Hoedemaeker, F. J. (2000) “1EXS: Structure Of Porcine Beta-Lactoglobulin”, Worldwide Protein Data Bank, p. 1EXS. doi: 10.2210/pdb1exs/pdb.   
McCoy, A. J., Jin, L., Abrahams, J.-P., Skinner, R. and Carrell, R. W. (2000) “1E03: Plasma Alpha Antithrombin-Iii And Pentasaccharide”, Worldwide Protein Data Bank, p. 1000. doi: 10.2210/pdb1e03/pdb.   
McCoy, A. J., Skinner, R., Abrahams, J.-P., Pei, X. Y. and Carrell, R. W. (2000) “1E04: Plasma Beta Antithrombin-Iii”, Worldwide Protein Data Bank, p. 10000. doi: 10.2210/pdb1e04/pdb.   
Elliott, P. R., Abrahams, J. P. and Lomas, D. A. (1999) “Crystal structure of wildtype alpha(1)-antitrypsin”, American Journal Of Respiratory And Critical Care Medicine. American Lung Association.   edoc
Pei, X. Y., Skinner, R., Abrahams, J. P. and Carrell, R. W. (1999) “2.6A Structure Of Preferentially Active Isoform Of Human Antithrombin”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography.   edoc
Hoedemaeker, F. J., Siegal, G., Roe, S. M., Driscoll, P. C. and Abrahams, J. P. (1999) “Crystal structure of the C-terminal SH2 domain of the p85 alpha regulatory subunit of phosphoinositide 3-kinase: An SH2 domain mimicking its own substrate”, Journal of Molecular Biology. Elsevier, 292(4), pp. 763–770. doi: 10.1006/jmbi.1999.3111.   edoc
Hoedemaeker, F. J., Siegal, G., Roe, S. M., Driscoll, P. C. and Abrahams, J. P. (1999) “Crystal structure of the C-terminal SH2 domain of the p85 alpha regulatory subunit of phosphoinositide 3-kinase: An SH2 domain mimicking its own substrate (vol 292, pg 763, 1999)”, Journal of Molecular Biology. Elsevier, 294(3), p. 825. doi: 10.1006/jmbi.1999.3337.   edoc
Leslie, A. G. W., Abrahams, J. P., Braig, K., Lutter, R., Menz, R. I., Orriss, G. L., van Raaij, M. J. and Walker, J. E. (1999) “The structure of bovine mitochondrial F-1-ATPase: an example of rotary catalysis”, Biochemical Society Transactions. Portland Press, 27(2), pp. 37–42. doi: 10.1042/bst0270037.   edoc
Jin, L., Abrahams, J. P., Skinner, R., Petitou, M., Pike, R. N. and Carrell, R. W. (1999) “1AZX: Antithrombin/Pentasaccharide Complex”, Worldwide Protein Data Bank, p. 1AZX. doi: 10.2210/pdb1azx/pdb.   
Abrahams, J. P. and De Graaff, R. A. G. (1998) “New developments in phase refinement”, Current Opinion in Structural Biology. Elsevier, 8(5), pp. 601–605. doi: 10.1016/S0959-440X(98)80151-6.   edoc
Elliott, P. R., Abrahams, J.-P. and Lomas, D. A. (1998) “Wild-type alpha(1)-antitrypsin is in the canonical inhibitory conformation”, Journal of Molecular Biology. Academic Press, 275(3), pp. 419–425. doi: 10.1006/jmbi.1997.1458.   edoc
Skinner, R., Chang, W.-S. W., Jin, L., Pei, X., Huntington, J. A., Abrahams, J.-P., Carrell, R. W. and Lomas, D. A. (1998) “Implications for function and therapy of a 2.9 å structure of binary-complexed antithrombin”, Journal of Molecular Biology. Elsevier, 283(1), pp. 9–14. doi: 10.1006/jmbi.1998.2083.   edoc
Skinner, R., Chang, W. S. W., Jin, L., Pei, X. Y., Huntington, J. A., Abrahams, J. P., Carrell, R. W. and Lomas, D. A. (1998) “1BR8: Implications For Function And Therapy Of A 2.9A Structure Of Binary-Complexed Antithrombin”, Worldwide Protein Data Bank, p. 1BR8. doi: 10.2210/pdb1br8/pdb.   
Shirakihara, Y., Leslie, A. G. W., Abrahams, J. P., Walker, J. E., Ueda, T., Sekimoto, Y., Kambara, M., Saika, K., Kagawa, Y. and Yoshida, M. (1998) “1SKY: Crystal Structure Of The Nucleotide Free Alpha3beta3 Sub-Complex Of F1-Atpase From The Thermophilic Bacillus Ps3”, Worldwide Protein Data Bank, p. 1SKY. doi: 10.2210/pdb1sky/pdb.   
Abrahams, J. P. (1997) “Bias reduction in phase refinement by modified interference functions: Introducing the gamma correction”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 53, pp. 371–376. doi: 10.1107/S0907444996015272.   edoc
Skinner, R., Abrahams, J.-P., Whisstock, J. C., Lesk, A. M., Carrell, R. W. and Wardell, M. R. (1997) “The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site”, Journal of Molecular Biology. Elsevier, 266(3), pp. 601–609. doi: 10.1006/jmbi.1996.0798.   edoc
Jin, L., Abrahams, J. P., Skinner, R., Petitou, M., Pike, R. N. and Carrell, R. W. (1997) “The anticoagulant activation of antithrombin by heparin”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 94(26), pp. 14683–14688. doi: 10.1073/pnas.94.26.14683.   edoc
Shirakihara, Y., Leslie, A. G. W., Abrahams, J. P., Walker, J. E., Ueda, T., Sekimoto, Y., Kambara, M., Saika, K., Kagawa, Y. and Yoshida, M. (1997) “The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F-1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer”, Structure. Cell Press, 5(6), pp. 825–836. doi: 10.1016/S0969-2126(97)00236-0.   edoc
Wardell, M. R., Skinner, R., Carter, D. C., Twigg, P. D. and Abrahams, J. P. (1997) “Improved diffraction of antithrombin crystals grown in microgravity”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 53, pp. 622–625. doi: 10.1107/S0907444997003302.   edoc
Carrell, R., Skinner, R., Jin, L. and Abrahams, J. P. (1997) “Structural mobility of antithrombin and its modulation by heparin”, Thrombosis and Haemostasis. Schattauer, 78(1), pp. 516–519.   edoc
Skinner, R., Abrahams, J.-P., Whisstock, J. C., Lesk, A. M., Carrell, R. W. and Wardell, M. R. (1997) “2ANT: The 2.6 A Structure Of Antithrombin Indicates A Conformational Change At The Heparin Binding Site”, Worldwide Protein Data Bank, p. 2ANT. doi: 10.2210/pdb2ant/pdb.   
Abrahams, J. P., Buchanan, S. K., Van Raaij, M. J., Fearnley, I. M., Leslie, A. G. W. and Walker, J. E. (1997) “1EFR: Bovine Mitochondrial F1-Atpase Complexed With The Peptide Antibiotic Efrapeptin”, Worldwide Protein Data Bank, p. 1EFR. doi: 10.2210/pdb1efr/pdb.   
Abrahams, J. P., Leslie, A. G. W., Lutter, R. and Walker, J. E. (1996) “The structure of bovine mitochondrial F1-ATPase - An insight into ATP synthesis”, Biophysical Journal. Cell Press.   edoc
Leslie, A. G. W., Abrahams, J. P., van Raaij, M., Lutter, R. and Walker, J. E. (1996) “The structure of bovine mitochondrial F1-ATPase - an example of rotational catalysis?”, Acta Crystallographica A-Foundation And Advances. International Union of Crystallography. doi: 10.1107/S010876739609890X.   edoc
van Raaij, M. J., Abrahams, J. P., Leslie, A. G. W. and Walker, J. E. (1996) “The structure of bovine F-1-ATPase complexed with the antibiotic inhibitor aurovertin B”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 93(14), pp. 6913–6917. doi: 10.1073/pnas.93.14.6913.   edoc
Abrahams, J. P. and Leslie, A. G. W. (1996) “Methods used in the structure determination of bovine mitochondrial F-1 ATPase”, Acta Crystallographica. Section D, Biological Crystallography. Munksgaard, 52, pp. 30–42. doi: 10.1107/S0907444995008754.   edoc
Abrahams, J. P., Buchanan, S. K., van Raaij, M. J., Fearnley, I. M., Leslie, A. G. W. and Walker, J. E. (1996) “The structure of bovine F-1-ATPase complexed with the peptide antibiotic efrapeptin”, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 93(18), pp. 9420–9424. doi: 10.1073/pnas.93.18.9420.   edoc
Elliott, P. R., Lomas, D. A., Carrell, R. W. and Abrahams, J. P. (1996) “Inhibitory conformation of the reactive loop of alpha(1)-antitrypsin”, Nature Structural biology. Nature Publishing Co, 3(8), pp. 676–681. doi: 10.1038/nsb0896-676.   edoc
Van Raaij, M., Abrahams, J. P., Leslie, A. G. W. and Walker, J. E. (1996) “1COW: Bovine Mitochondrial F1-Atpase Complexed With Aurovertin B”, Worldwide Protein Data Bank, p. 1COW. doi: 10.2210/pdb1cow/pdb.   
Abrahams, J. P., Leslie, A. G. W., Lutter, R. and Walker, J. E. (1996) “1BMF: Bovine Mitochondrial F1-Atpase”, Worldwide Protein Data Bank, p. 1BMF. doi: 10.2210/pdb1bmf/pdb.   
Abrahams, J. P., Elliott, P. R., Lomas, D. A. and Carrell, R. W. (1996) “1PSI: Intact recombined alpha1-antitrypsin mutant PHE 51 to LEU”, Worldwide Protein Data Bank, p. 1PSI. doi: 10.2210/pdb1psi/pdb.   
Abrahams, J. P., Leslie, A. G. W., Lutter, R. and Walker, J. E. (1994) “Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria”, Nature. Nature Research, 370(6491), pp. 621–628. doi: 10.1038/370621a0.   edoc
Abrahams, J. P., Lutter, R., Todd, R. J., Van Raaij, M. J., Leslie, A. G. W. and Walker, J. E. (1993) “Inherent asymmetry of the structure of F1‐ATPase from bovine heart mitochondria at 6.5 A resolution”, The EMBO journal. EMBO Press, 12(5), pp. 1775–1780. doi: 10.1002/j.1460-2075.1993.tb05825.x.   edoc
Wardell, M. R., Abrahams, J.-P., Bruce, D., Skinner, R. and Leslie, A. G. W. (1993) “Crystallization and Preliminary X-ray Diffraction Analysis of Two Conformations of Intact Human Antithrombin”, Journal of Molecular Biology. Elsevier, 234(4), pp. 1253–1258. doi: 10.1006/jmbi.1993.1676.   edoc
Lutter, R., Abrahams, J. P., Van Raaij, M. J., Todd, R. J., Lundqvist, T., Buchanan, S. K., Leslie, A. G. W. and Walker, J. E. (1993) “Crystallization of F1-ATPase from Bovine Heart Mitochondria”, Journal of Molecular Biology. Elsevier, 229(3), pp. 787–790. doi: 10.1006/jmbi.1993.1081.   edoc
Abrahams, J. P., Bosch, L., Kraal, B., De Groot, H. J. M., Raap, J. and Lugtenburg, J. (1992) “Magic angle spinning carbon-13 NMR analysis of the complex of elongation factor Tu, GTP and (1-carbon-13) phenylalanyl-tRNA-Phe”, Spectroscopy (Amsterdam), 10(1-6), pp. 1–8.   
Abrahams, J. P., Acampo, J. J. C., Kraal, B. and Bosch, L. (1991) “The influence of tRNA located at the P-site on the turnover of EF-Tu·GTP on ribosomes ”, Biochimie. Elsevier, 73(7-8), pp. 1089–1092. doi: 10.1016/0300-9084(91)90150-Y.   edoc
Abrahams, J. P., Kraal, B., Clark, B. F. C. and Bosch, L. (1991) “Isolation and stability of ternary complexes of elongation factor Tu, GTP and aminoacyl-tRNA ”, Nucleic Acids Research. Oxford University Press, 19(3), pp. 553–556. doi: 10.1093/nar/19.3.553.   edoc
Abrahams, J. P., Van Raaij, M. J., Ott, G., Kraal, B. and Bosch, L. (1991) “Kirromycin drastically reduces the affinity of Escherichia coli elongation factor Tu for aminoacyl-tRNA”, Biochemistry. American Chemical Society, 30(27), pp. 6705–6710. doi: 10.1021/bi00241a010.   edoc
Abrahams, J. P., Acampo, J. J. C., Ott, G., Sprinzl, M., Degraaf, J. M., Talens, A. and Kraal, B. (1990) “THE INTERACTION BETWEEN AMINOACYL-TRANSFER RNA AND THE MUTANT ELONGATION FACTOR-TUAR AND FACTOR-TUBO”, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Elsevier, 1050(1-3), pp. 226–229. doi: 10.1016/0167-4781(90)90171-W.   edoc
Abrahams, J. P., Vandenberg, M., Van Batenburg, E. and Pleij, C. (1990) “Prediction of RNA secondary structure, including pseudoknotting, by computer simulation”, Nucleic Acids Research. Oxford University Press, 18(10), pp. 3035–3044. doi: 10.1093/nar/18.10.3035.   edoc
Kraal, B., Abrahams, J. P. and Bosch, L. (1989) “Effects Of Kirromycin On The Elongation Factor-Ef-Tu And Its Interactions With Gdp Or Gtp And Transfer-Rna - The Application Of Zone-Interference Gel-Electrophoresis, A New Method For The Analysis Of Weak Complexes”, in Bosch, L., Kraal, B., and Parmeggiani, A. (eds.) The guanine-nucleotide binding proteins. Common structural and functional properties. New York: Plenum Press (NATO ASI series. Series A, Life sciences, 165), pp. 121–129.   edoc
Abrahams, J. P., Kraal, B. and Bosch, L. (1988) “Zone-interference gel electrophoresis: a new method for studying weak protein-nucleic acid complexes under native equilibrium conditions”, Nucleic Acids Research. Oxford University Press, 16(21), pp. 10099–10108. doi: 10.1093/nar/16.21.10099.   edoc
Pleij, C. W. A., Abrahams, J. P., Van Belkum, A., Rietveld, K. and Bosch, L. (1986) “The Spatial Folding Of The 3’ Noncoding Region Of Aminoacylatable Plant Viral RNAs”, Journal of Cellular Biochemistry. Wiley.   edoc
Van Belkum, A., Abrahams, J. P., Pleij, C. W. A. and Bosch, L. (1985) “Five pseudoknots are present at the 204 nucleotides long 3’ noncoding region of tobacco mosak virus RNA”, Nucleic Acids Research. Oxford University Press, 13(21), pp. 7673–7686. doi: 10.1093/nar/13.21.7673.   edoc