Koning, R., van den Worm, S., Plaisier, J.R., van Duin, J., Abrahams, J.P., Koerten, H. , Visualization by cryo-electron microscopy of genomic RNA that binds to the protein capsid inside bacteriophage MS2, Journal of Molecular Biology, vol. 332, no. 2, pp. 415-422. DOI

Zhang, Y.H., Leliveld, S.R., Kooistra, K., Molenaar, C., Rohn, J.L., Tanke, H.J., Abrahams, J.P., Noteborn, M.H.M. , Recombinant Apoptin multimers kill tumor cells but are nontoxic and epitope-shielded in a normal-cell-specific fashion, Experimental Cell Research, vol. 289, no. 1, pp. 36-46. DOI

Rutjes, S.A., Bosma, P.J., Rohn, J.L., Noteborn, M.H.M., Wesseling, J.G. , Induction of insolubility by herpes simplex virus VP22 precludes intercellular trafficking of N-terminal Apoptin-VP22 fusion proteins, Journal of Molecular Medicine-Jmm, vol. 81, no. 9, pp. 558-565. DOI

Leliveld, S.R., Noteborn, M.H.M., Abrahams, J.P. , Prevalent conformations and subunit exchange in the biologically active apoptin protein multimer, European Journal of Biochemistry, vol. 270, no. 17, pp. 3619-3627. DOI

Pannu, N.S., McCoy, A.J., Read, R.J. , Application of the complex multivariate normal distribution to crystallographic methods with insights into multiple isomorphous replacement phasing, Acta Crystallographica Section D-Biological Crystallography, vol. 59, pp. 1801-1808. DOI

Leliveld, S.R., Zhang, Y.H., Rohn, J.L., Noteborn, M.H.M., Abrahams, J.P. , Apoptin induces tumor-specific apoptosis as a globular multimer, Journal of Biological Chemistry, vol. 278, no. 11, pp. 9042-9051. DOI

Hilge, M., Siegal, G., Vuister, G.W., Guntert, P., Gloor, S.M., Abrahams, J.P. , ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase, Nature Structural Biology, vol. 10, no. 6, pp. 468-474. DOI

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., Noteborn, M.H.M. , Importance of nuclear localization of apoptin for tumor-specific induction of apoptosis, Journal of Biological Chemistry, vol. 278, no. 30, pp. 27729-27736. DOI

van Roon, A.M.M., Pannu, N.S., Hokke, C.H., Deelder, A.M., Abrahams, J.P. , Crystallization and preliminary X-ray analysis of an anti-LewisX Fab fragment with and without its LewisX antigen, Acta Crystallographica Section D-Biological Crystallography, vol. 59, pp. 1306-1309. DOI

McCoy, A.J., Pei, X.Y., Skinner, R., Abrahams, J.P., Carrell, R.W. , Structure of beta-antithrombin and the effect of glycosylation on antithrombin's heparin affinity and activity, Journal of Molecular Biology, vol. 326, no. 3, pp. 823-833. DOI

Thomassen, E., Gielen, G., Schutz, M., Schoehn, G., Abrahams, J.P., Miller, S., van Raaij, M.J. , 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, vol. 331, no. 2, pp. 361-373. DOI

Bos, I.G.A., Lubbers, Y.T.P., Roem, D., Abrahams, J.P., Hack, C.E., Eldering, E. , 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, vol. 278, no. 32, pp. 29463-29470. DOI

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., Abrahams, J.P. , Area detectors in structural biology, Nuclear Instruments & Methods in Physics Research Section a-Accelerators Spectrometers Detectors and Associated Equipment, vol. 509, no. 1-3, pp. 274-282. DOI

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., Abrahams, J.P. , Apoptin protein multimers form distinct higher-order nucleoprotein complexes with DNA, Nucleic Acids Research, vol. 31, no. 16, pp. 4805-4813. DOI

Abrahams, J.P., Thomassen, E.A.J. , Mechanism of thrombin's enigmatic sodium switch revealed, Structure, vol. 11, no. 4, pp. 363-364. DOI

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Schmauder, R., Schmidt, T., Abrahams, J.P., Kuil, M.E. , Screening crystallisation conditions using fluorescence correlation spectroscopy, Acta Crystallographica Section D-Biological Crystallography, vol. 58, pp. 1536-1541. DOI

Bodenstaff, E.R., Hoedemaeker, F.J., Kuil, M.E., de Vrind, H.P.M., Abrahams, J.P. , The prospects of protein nanocrystallography, Acta Crystallographica Section D-Biological Crystallography, vol. 58, pp. 1901-1906. DOI

Kuil, M.E., Bodenstaff, E.R., Hoedemaeker, F.J., Abrahams, J.P. , Protein nano-crystallogenesis, Enzyme and Microbial Technology, vol. 30, no. 3, pp. 262-265. DOI

Mitraki, A., Miller, S., van Raaij, M.J. , Review: Conformation and folding of novel beta-structural elements in viral fiber proteins: The triple beta-spiral and triple beta-helix, Journal of Structural Biology, vol. 137, no. 1-2, pp. 236-247. DOI

Schmauder, R., Schmidt, T., Abrahams, J.P., Kuil, M.E. , Screening Crystallisation conditions using Fluorescence Correlation Spectroscopy, Acta Crystallographica Section D-Biological Crystallography, vol. 58, issue 1, pp. 1536-1541. DOI

Bos, I.G.A., Hack, C.E., Abrahams, J.P. , Structural and functional aspects of C1-Inhibitor, Immunobiology, vol. 205, issue 4-5, no. 4-5: Urban & Fischer Verlag, Branch Office Jena, P O BOX 100537, D-07705 JENA, GERMANY , pp. 518-533.

Hoedemaeker, F.J., Visschers, R.W., Alting, A.C., de Kruif, K.G., Kuil, M.E., Abrahams, J.P. , A novel pH-dependent dimerization motif in beta-lactoglobulin from pig (Sus scrofa), Acta Crystallographica Section D-Biological Crystallography, vol. 58, pp. 480-486.

Lortat-Jacob, H., Chouin, E., Cusack, S., van Raaij, M.J. , Kinetic analysis of adenovirus fiber binding to its receptor reveals an avidity mechanism for trimeric receptor-ligand interactions, Journal of Biological Chemistry, vol. 276, no. 12, pp. 9009-9015.

van Raaij, M.J., Schoehn, G., Jaquinod, M., Ashman, K., Burda, M.R., Miller, S. , Identification and crystallisation of a heat- and protease-stable fragment of the bacteriophage T4 short tail fibre, Biological Chemistry, vol. 382, no. 7, pp. 1049-1055.