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Laboratory for Nanoscale Biology

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Prof. Dr. Jan Pieter Abrahams

Photo of Jan Pieter Abrahams
Paul Scherrer Institute
Forschungsstrasse 111
5232 Villigen PSI
Switzerland
Telephone
+41 56 310 46 12
Email
jan-pieter.abrahams@psi.ch

Personal Information - CV and Publication List

Download Curriculum Vitae and Publication List


Group Research

To comprehend how matter creates life requires visualising the living cell in atomic detail. To this aim, we develop novel technologies that are based on electron diffraction of frozen, hydrated biological samples. We have demonstrated (using biological and organic nano-crystals) that electron diffraction data can in principle unlock high-resolution information way beyond what conventional electron microscopy can deliver, and that this also applies to other biological samples. To exploit this novel approach in the study of cellular processes, we scan samples with a coherent beam with a diameter down to several nanometers, and measure the diffracted electrons using modern hybrid pixel detectors as developed by PSI’s detector group. For phasing of these data, we develop a range of methods that combine experimental and computational approaches. We apply our research to the study of the molecular response to mitochondrial stress central to neuro-degeneration and aging.

Group Members

Photo of Jan Pieter Abrahams
Prof. Dr. Jan Pieter Abrahams
+41 56 310 46 12
jan-pieter.abrahams@psi.ch
Photo of Eric van Genderen
Dr. Eric van Genderen

Scientist

+41 56 310 46 19
eric.van-genderen@psi.ch
Tatiana_Latychevskaia
PD Dr. Tatiana Latychevskaia

Scientist

+41 56 310 46 79
tatiana.latychevskaia@psi.ch
Photo of Thorsten Blum
Dr. Thorsten Blum

Postdoc

+41 56 310 54 22
thorsten.blum@psi.ch
Photo of Pooja Thakkar
Pooja Thakkar

Ph.D. Student

+41 56 310 39 22
pooja.thakkar@psi.ch

Group Publications

2019

  • Nuclear Pore Membrane Proteins Self-Assemble into Nanopores Panatala R, Barbato S, Kozai T, Luo J, Kapinos Larisa E, Lim Roderick YH
    BIOCHEMISTRY 58, 484 (2019).
    DOI: 10.1021/acs.biochem.8b01179(link is external)

2018

  • Electron crystallography with the EIGER detector Tinti G, Fröjdh E, van Genderen E, Gruene T, Schmitt B, de Winter MDA, Weckhuysen BM, Abrahams J
    IUCRJ 5, 190 (2018).
    DOI: 10.1107/S2052252518000945
  • Frontispiece: Characterization at the Level of Individual Crystals: Single-Crystal MFI Type Zeolite Grains Gruene T, Li T, van Genderen E, Pinar Ana B, van Bokhoven JA
    CHEMISTRY - A EUROPEAN JOURNAL 24, 2384 (2018).
    DOI: 10.1002/chem.201881065

2017

  • Characterization at the level of individual crystals: single crystal MFI type zeolite grains Gruene T, Li T, van Genderen E, Pinar AB, van Bokhoven JA
    CHEMISTRY - A EUROPEAN JOURNAL 24, 2384 (2017).
    DOI: 10.1002/chem.201704213
  • Protein structure determination by electron diffraction using a single three-dimensional nanocrystal Clabbers MTB, van Genderen E, Wan W, Wiegers EL, Gruene T, Abrahams JP
    Acta Crystallographica Section D Structural Biology 73, 738 (2017).
    DOI: 10.1107/S2059798317010348

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 van Genderen E, Clabbers MTB, Das PP, Stewart A, Nederlof I, Barentsen KC, Portillo Q, Pannu NS, Nicolopoulos S, Gruene T, Abrahams JP
    Acta Crystallographica Section A Foundations and Advances 72, 236 (2016).
    DOI: 10.1107/S2053273315022500
  • Characterization of Mn(II) ion binding to the amyloid-? peptide in Alzheimer?s disease Wallin C, Kulkarni Yashraj S, Abelein A, Jarvet J, Liao Q, Strodel B, Olsson L, Luo J, Abrahams J, Sholts Sabrina B, Roos Per M, Kamerlin Shina CL, Gräslund A, Wärmländer Sebastian KTS
    JOURNAL OF TRACE ELEMENTS IN MEDICINE AND BIOLOGY , (2016).
    DOI: 10.1016/j.jtemb.2016.03.009
  • Cross-interactions between the Alzheimer Disease Amyloid-? Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
    JOURNAL OF BIOLOGICAL CHEMISTRY 291, 16485 (2016).
    DOI: 10.1074/jbc.R116.714576
  • Lattice filter for processing image data of three-dimensional protein nanocrystals van Genderen E, Li YW, Nederlof I, Abrahams JP
    ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 72, 34 (2016).
    DOI: 10.1107/S205979831502149X
  • Modern X-ray analysis on single crystals - a practical guide Gruene T
    Crystallography Reviews 22, 287 (2016).
    DOI: 10.1080/0889311X.2016.1237508
  • Reciprocal Molecular Interactions between the A? Peptide Linked to Alzheimer?s Disease and Insulin Linked to Diabetes Mellitus Type II Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
    ACS Chemical Neuroscience 7, 269 (2016).
    DOI: 10.1021/acschemneuro.5b00325

2015

  • A posteriori correction of camera characteristics from large image data sets Afanasyev P, Ravelli Raimond BG, Matadeen R, De Carlo S, van Duinen G, Alewijnse B, Peters Peter J, Abrahams J, Portugal Rodrigo V, Schatz M, van Heel M
    Scientific Reports 5, 10317 (2015).
    DOI: 10.1038/srep10317
  • Electron crystallography of 3D nano-crystals Clabbers Max TB, van Genderen E, Nederlof I, Li Y, Abrahams J
    Acta Crystallographica Section A Foundations and Advances 71, s405 (2015).
    DOI: 10.1107/S2053273315093985
  • Electron diffraction and imaging of 3D nanocrystals of pharmaceuticals, peptides and proteins Abrahams J, van Genderen E, Nederlof I, Clabbers M, Li Y
    Acta Crystallographica Section A Foundations and Advances 71, s103 (2015).
    DOI: 10.1107/S2053273315098496

2014

  • Alzheimer Peptides Aggregate into Transient Nanoglobules That Nucleate Fibrils Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
    BIOCHEMISTRY 53, 6302 (2014).
    DOI: 10.1021/bi5003579
  • ChemInform Abstract: Cyclic Peptides as Inhibitors of Amyloid Fibrillation Luo J, Abrahams J
    ChemInform 45, no (2014).
    DOI: 10.1002/chin.201422265
  • Cyclic Peptides as Inhibitors of Amyloid Fibrillation Luo J, Abrahams J
    CHEMISTRY - A EUROPEAN JOURNAL 20, 2410 (2014).
    DOI: 10.1002/chem.201304253
  • Endogenous Polyamines Reduce the Toxicity of Soluble A? Peptide Aggregates Associated with Alzheimer?s Disease Luo J, Mohammed I, Wärmländer Sebastian KTS, Hiruma Y, Gräslund A, Abrahams J
    BIOMACROMOLECULES 15, 1985 (2014).
    DOI: 10.1021/bm401874j
  • Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid ? Peptide Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
    JOURNAL OF BIOLOGICAL CHEMISTRY 289, 27766 (2014).
    DOI: 10.1074/jbc.M114.574947
  • The A- peptide forms non-amyloid fibrils in the presence of carbon nanotubes Luo J, Waermlaender Sebastian KTS, Yu C, Muhammad K, Graeslund A, Abrahams JP
    NANOSCALE 6, 6720 (2014).
    DOI: 10.1039/c4nr00291a
  • The hairpin conformation of the amyloid ? peptide is an important structural motif along the aggregation pathway Abelein A, Abrahams J, Danielsson J, Gräslund A, Jarvet J, Luo J, Tiiman A, Wärmländer Sebastian KTS
    JBIC JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY 19, 623 (2014).
    DOI: 10.1007/s00775-014-1131-8

2013

  • A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals Nederlof I, van Genderen E, Li Y, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 69, 1223 (2013).
    DOI: 10.1107/S0907444913009700
  • An efficient nanolitre-volume multi-channel device for highly viscous materials used in membrane protein crystallization Luo J, Zwier R, Abrahams J
    JOURNAL OF APPLIED CRYSTALLOGRAPHY 46, 829 (2013).
    DOI: 10.1107/S0021889813006742
  • Capture of unstable protein complex on the streptavidin-coated single-walled carbon nanotubes Liu Z, Voskamp P, Zhang Y, Chu F, Abrahams J
    JOURNAL OF NANOPARTICLE RESEARCH 15, (2013).
    DOI: 10.1007/s11051-013-1582-9
  • Cellular Polyamines Promote Amyloid-Beta (A?) Peptide Fibrillation and Modulate the Aggregation Pathways Luo J, Yu C, Yu H, Borstnar R, Kamerlin Shina CL, Gräslund A, Abrahams J, Wärmländer Sebastian KTS
    ACS Chemical Neuroscience 4, 454 (2013).
    DOI: 10.1021/cn300170x
  • Human lysozyme inhibits the in vitro aggregation of A? peptides, which in vivo are associated with Alzheimer's disease Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
    CHEMICAL COMMUNICATIONS 49, 6507 (2013).
    DOI: 10.1039/c3cc42325e
  • Imaging protein three-dimensional nanocrystals with cryo-EM Nederlof I, Li Y, van Heel M, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 69, 852 (2013).
    DOI: 10.1107/S0907444913002734
  • Visualizing the localization of transfection complexes during graphene nanoparticle-based transfection Bruggencate F, Laroche F, Zhang Y, Song G, Yin S, Abrahams J, Liu Z
    JOURNAL OF MATERIALS CHEMISTRY B 1, 6353 (2013).
    DOI: 10.1039/C3TB21349H

2012

  • Characterisation of a counting imaging detector for electron detection in the energy range 10?20keV Moldovan G, Sikharulidze I, Matheson J, Derbyshire G, Kirkland AI, Abrahams JP
    Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Dectectors and Associated Equipment 681, 21 (2012).
    DOI: 10.1016/j.nima.2012.03.033
  • Single-Walled Carbon Nanotubes as Scaffolds to Concentrate DNA for the Study of DNA-Protein Interactions Liu Z, Galli F, Waterreus W, Meulenbroek E, Koning Roman I, Lamers Gerda EM, Olsthoorn René CL, Pannu N, Oosterkamp TjerkH, Koster Abraham J, Dame Remus T, Abrahams J
    CHEMPHYSCHEM 13, 1569 (2012).
    DOI: 10.1002/cphc.201100896
  • Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato Meulenbroek Elisabeth M, Thomassen Ellen AJ, Pouvreau L, Abrahams J, Gruppen H, Pannu Navraj S
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 68, 794 (2012).
    DOI: 10.1107/S090744491201222X
  • Ultra-small graphene oxide functionalized with polyethylenimine (PEI) for very efficient gene delivery in cell and zebrafish embryos Zhou X, Laroche F, Lamers Gerda EM, Torraca V, Voskamp P, Lu T, Chu F, Spaink Herman P, Abrahams J, Liu Z
    Nano Research 5, 703 (2012).
    DOI: 10.1007/s12274-012-0254-x

2011

  • A Straightforward and Robust Method for Introducing Human Hair as a Nucleant into High Throughput Crystallization Trials Nederlof I, Hosseini R, Georgieva D, Luo J, Li D, Abrahams J
    CRYSTAL GROWTH & DESIGN 11, 1170 (2011).
    DOI: 10.1021/cg101374r
  • Advances in the CRANK software suite for automated crystal structure solution Waterreus WJ, Skubák P, Sikharulidze I, Abrahams JP, de Graaff RAG, Pannu NS
    Acta Crystallographica Section A Foundations of Crystallography 67, C659 (2011).
    DOI: 10.1107/S0108767311083346
  • EDIFF : a program for automated unit-cell determination and indexing of electron diffraction data Jiang L, Georgieva D, Abrahams J
    JOURNAL OF APPLIED CRYSTALLOGRAPHY 44, 1132 (2011).
    DOI: 10.1107/S0021889811030731
  • Electron diffraction of submicron three-dimensional protein crystals Nederlof I, Georgieva D, Abrahams JP
    Acta Crystallographica Section A Foundations of Crystallography 67, C228 (2011).
    DOI: 10.1107/S010876731109430X
  • IMPROVED IMAGING IN LOW ENERGY ELECTRON MICROSCOPY AND PHOTO EMISSION ELECTRON MICROSCOPY USING MEDIPIX2 PIXEL DETECTOR SIKHARULIDZE I, van GASTEL R, SCHRAMM S, ABRAHAMS JP, POELSEMA B, TROM RM, van der MOLEN SJ
    Astroparticle, Particle and Space Physics, Detectors and Medical Physics Applications , (2011).
    DOI: 10.1142/9789814307529_0023
  • Image Processing and Lattice Determination for Three-Dimensional Nanocrystals Jiang L, Georgieva D, Nederlof I, Liu Z, Abrahams J
    MICROSCOPY AND MICROANALYSIS 17, 879 (2011).
    DOI: 10.1017/S1431927611012244
  • Low energy electron microscopy imaging using Medipix2 detector Sikharulidze I, van Gastel R, Schramm S, Abrahams JP, Poelsema B, Tromp RM, van der Molen SJ
    Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Dectectors and Associated Equipment 633, S239 (2011).
    DOI: 10.1016/j.nima.2010.06.177
  • Low-resolution electron crystallography challenges in organic and inorganic crystals with transmission electron microscope (TEM) Nicolopoulos S, Rauch E, Georgieva D, Abrahams JP
    Acta Crystallographica Section A Foundations of Crystallography 67, C188 (2011).
    DOI: 10.1107/S0108767311095304
  • Recent advances in the CRANK software suite for experimental phasing Pannu Navraj S, Waterreus W, Skubák P, Sikharulidze I, Abrahams J, de Graaff Rudolf AG
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 67, 331 (2011).
    DOI: 10.1107/S0907444910052224

2010

  • A Graphene Oxide?Streptavidin Complex for Biorecognition - Towards Affinity Purification Liu Z, Jiang L, Galli F, Nederlof I, Olsthoorn René CL, Lamers Gerda EM, Oosterkamp TjerkH, Abrahams J
    ADVANCED FUNCTIONAL MATERIALS 20, 2857 (2010).
    DOI: 10.1002/adfm.201000761
  • A novel approximation method of CTF amplitude correction for 3D single particle reconstruction Jiang L, Liu Z, Georgieva D, Kuil Maxim E, Abrahams J
    ULTRAMICROSCOPY 110, 350 (2010).
    DOI: 10.1016/j.ultramic.2010.01.011
  • Stable Single-Walled Carbon Nanotube-Streptavidin Complex for Biorecognition Liu Z, Galli F, Janssen Kjeld GH, Jiang L, van der Linden Heiko J, de Geus Daniel C, Voskamp P, Kuil Maxim E, Olsthoorn Rene CL, Oosterkamp TjerkH, Hankemeier T, Abrahams J
    JOURNAL OF PHYSICAL CHEMISTRY C 114, 4345 (2010).
    DOI: 10.1021/jp911441d
  • The strong phase object approximation may allow extending crystallographic phases of dynamical electron diffraction patterns of 3D protein nano-crystals Abrahams J
    ZEITSCHRIFT FUR KRISTALLOGRAPHIE 225, (2010).
    DOI: 10.1524/zkri.2010.1216

2009

  • An Intelligent Peak Search Program for Digital Electron Diffraction Images of 3D Nano-Crystals Jiang L, Georgieva D, IJspeert K, Abrahams J
    2009 2nd International Congress on Image and Signal Processing , (2009).
    DOI: 10.1109/CISP.2009.5301421
  • Characterization of a diagnostic Fab fragment binding trimeric Lewis X de Geus Daniël C, van Roon AnneMarie M, Thomassen Ellen AJ, Hokke Cornelis H, Deelder André M, Abrahams J
    PROTEINS: STRUCTURE, FUNCTION, AND BIOINFORMATICS 76, 439 (2009).
    DOI: 10.1002/prot.22356
  • Crystal Structure of Chlorite Dismutase, a Detoxifying Enzyme Producing Molecular Oxygen de Geus Daniël C, Thomassen Ellen AJ, Hagedoorn P, Pannu Navraj S, van Duijn E, Abrahams J
    JOURNAL OF MOLECULAR BIOLOGY 387, 192 (2009).
    DOI: 10.1016/j.jmb.2009.01.036
  • Involvement of a carboxylated lysine in UV damage endonuclease Meulenbroek Elisabeth M, Paspaleva K, Thomassen Ellen AJ, Abrahams J, Goosen N, Pannu Navraj S
    PROTEIN SCIENCE 18, 549 (2009).
    DOI: 10.1002/pro.54
  • Macromolecular electron crystallography Abrahams J, Jiang L, Sikhuralidze I, Nederloff I, Zandbergen H, Georgieva D
    Acta Crystallographica Section A Foundations of Crystallography 65, s7 (2009).
    DOI: 10.1107/S0108767309099875
  • Mammalian Navigators are microtubule plus-end tracking proteins that can reorganize the cytoskeleton to induce neurite-like extensions van Haren J, Draegestein K, Keijzer N, Abrahams J, Grosveld F, Peeters P, Moechars D, Galjart N
    Cell Motility and the Cytoskeleton 66, 824 (2009).
    DOI: 10.1002/cm.20370
  • Medipix 2 detector applied to low energy electron microscopy van Gastel R, Sikharulidze I, Schramm S, Abrahams JP, Poelsema B, Tromp RM, van der Molen SJ
    ULTRAMICROSCOPY 110, 33 (2009).
    DOI: 10.1016/j.ultramic.2009.09.002
  • Recent advances in CRANK Waterreus W, Pannu N, Skubák P, Sikharulidze I, Abrahams J, de Graaff RAG
    Acta Crystallographica Section A Foundations of Crystallography 65, s160 (2009).
    DOI: 10.1107/S0108767309096743
  • Recycling of Aborted Ribosomal 50S Subunit-Nascent Chain-tRNA Complexes by the Heat Shock Protein Hsp15 Jiang L, Schaffitzel C, Bingel-Erlenmeyer R, Ban N, Korber P, Koning Roman I, de Geus Daniël C, Plaisier Jasper R, Abrahams J
    JOURNAL OF MOLECULAR BIOLOGY 386, 1357 (2009).
    DOI: 10.1016/j.jmb.2008.10.079
  • The Max-Inf2/Lorentz Center workshop on New algorithms in macromolecular crystallography and electron microscopy Pannu Navraj S, Ravelli Raimond BG, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 65, 623 (2009).
    DOI: 10.1107/S0907444909020861
  • Unit-cell determination from randomly oriented electron-diffraction patterns Jiang L, Georgieva D, Zandbergen Henny W, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 65, 625 (2009).
    DOI: 10.1107/S0907444909003163

2008

  • Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of chlorite dismutase: a detoxifying enzyme producing molecular oxygen de Geus Daniël C, Thomassen Ellen AJ, van der Feltz Clarisse L, Abrahams J
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 64, 730 (2008).
    DOI: 10.1107/S1744309108020551
  • Microtubule Plus-End Conformations and Dynamics in the Periphery of Interphase Mouse Fibroblasts Zovko S, Abrahams JP, Koster AJ, Galjart N, Mommaas AM
    MOLECULAR BIOLOGY OF THE CELL 19, 3138 (2008).
    DOI: 10.1091/mbc.E07-07-0681
  • Prospects for structure solution by electron diffraction of three-dimensional protein crystals Abrahams JP, Georgieva D, Jiang L, Zandbergen HW
    Acta Crystallographica Section A Foundations of Crystallography 64, C75 (2008).
    DOI: 10.1107/S0108767308097584

2007

  • Crystal Structure of the DNA Repair Enzyme Ultraviolet Damage Endonuclease Paspaleva K, Thomassen E, Pannu Navraj S, Iwai S, Moolenaar Geri F, Goosen N, Abrahams J
    STRUCTURE 15, 1316 (2007).
    DOI: 10.1016/j.str.2007.05.010
  • Cyclops: New modular software suite for cryo-EM Plaisier JR, Jiang L, Abrahams JP
    JOURNAL OF STRUCTURAL BIOLOGY 157, 19 (2007).
    DOI: 10.1016/j.jsb.2006.07.002
  • Heterogeneous nucleation of three-dimensional protein nanocrystals Georgieva Dilyana G, Kuil Maxim E, Oosterkamp Tjerk H, Zandbergen Henny W, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 63, 564 (2007).
    DOI: 10.1107/S0907444907007810
  • Recent advances in the CRANK automated structure solution suite Pannu NS, Skubak P, Sikharulidze I, Abrahams JP, de Graaff RAG
    Acta Crystallographica Section A Foundations of Crystallography 63, s116 (2007).
    DOI: 10.1107/S0108767307097516
  • Solving Ab-initio Protein and Nanostructures with Precession Electron Diffraction Georgieva D, Abrahams J, Zandbergen H, Nikolopoulos S, Boulahya K
    MICROSCOPY AND MICROANALYSIS 13, (2007).
    DOI: 10.1017/S1431927607072698
  • Structure of the E. coli signal recognition particle bound to a translating ribosome Schaffitzel C, Oswald M, Berger I, Ishikawa T, Abrahams J, Koerten Henk K, Koning Roman I, Ban N
    NATURE 448, 1076 (2007).
    DOI: 10.1038/nature06169

2006

  • Nano-dispensing by electrospray for biotechnology Kuil Maxim E, Abrahams J, Marijnissen Jan CM
    Biotechnology Journal 1, 969 (2006).
    DOI: 10.1002/biot.200600062
  • Structure of the E. coli signal recognition particle bound to a translating ribosome Schaffitzel C, Oswald M, Berger I, Ishikawa T, Abrahams J, Koerten Henk K, Koning Roman I, Ban N
    NATURE 444, 503 (2006).
    DOI: 10.1038/nature05182
  • The Impact of Single Amino Acid Substitutions in CD3? on the CD3?? Interaction and T-Cell Receptor?CD3 Complex Formation Thomassen EAJ, Dekking EHA, Thompson A, Franken KL, Sanal Ö, Abrahams JP, van Tol MJD, Koning F
    HUMAN IMMUNOLOGY 67, 579 (2006).
    DOI: 10.1016/j.humimm.2006.04.015

2005

  • The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin Thomassen Ellen AJ, Veen Harrie Avan, Berkel Patrick HCvan, Nuijens Jan H, Abrahams J
    TRANSGENIC RESEARCH 14, 397 (2005).
    DOI: 10.1007/s11248-005-3233-0

2004

  • CRANK - new methods for automated structure solution Ness S, de Graaff RAG, Abrahams JP, Pannu NS
    Acta Crystallographica Section A Foundations of Crystallography 60, s16 (2004).
    DOI: 10.1107/S0108767304099702
  • Crystal Structure of an Empty Capsid of Turnip Yellow Mosaic Virus van Roon AnneMarie M, Bink Hugo HJ, Plaisier Jasper R, Pleij Cornelis WA, Abrahams J, Pannu Navraj S
    JOURNAL OF MOLECULAR BIOLOGY 341, 1205 (2004).
    DOI: 10.1016/j.jmb.2004.06.085
  • Crystallization and preliminary X-ray crystallographic studies on a Kunitz-type potato serine protease inhibitor Thomassen Ellen AJ, Pouvreau L, Gruppen H, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 60, 1464 (2004).
    DOI: 10.1107/S0907444904013484
  • Effect of reactive site loop elongation on the inhibitory activity of C1-inhibitor Bos IGA, Lubbers YTP, Eldering E, Abrahams JP, Hack CE
    Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 1699, 139 (2004).
    DOI: 10.1016/j.bbapap.2004.02.006
  • Relevance of Apoptin's Integrity for Its Functional Behavior Rohn JL, Zhang YH, Leliveld SR, Danen-van Oorschot AAAM, Henriquez NV, Abrahams JP, Noteborn MHM
    JOURNAL OF VIROLOGY 79, 1337 (2004).
    DOI: 10.1128/JVI.79.2.1337-1338.2005
  • Structure of an Anti-Lewis X Fab Fragment in Complex with Its Lewis X Antigen van Roon A, Pannu N, de Vrind Johannes PM, van der Marel G, van Boom J, Hokke C, Deelder A, Abrahams J
    STRUCTURE 12, 1227 (2004).
    DOI: 10.1016/j.str.2004.05.008
  • TYSON: Robust searching, sorting, and selecting of single particles in electron micrographs Plaisier J, Leliveld SR, Kooistraa K, Molenaarc C, Rohan JL, Tanker HJ, Abrahams JP, Noteborn MHM
    JOURNAL OF STRUCTURAL BIOLOGY 145, 76 (2004).
    DOI: 10.1016/j.jsb.2003.09.030

2003

  • ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase Hilge M, Siegal G, Vuister G, Güntert P, Gloor S, Abrahams J
    Nature Structural Biology 10, 468 (2003).
    DOI: 10.1038/nsb924
  • Apoptin protein multimers form distinct higher-order nucleoprotein complexes with DNA Leliveld SR, Dame RT, Kommas MA, Koerten HK, Wyman C, Danen-van Oorschot AAAM, Rohn JL, Noteborn MHM, Abrahams JP
    NUCLEIC ACIDS RESEARCH 31, 4805 (2003).
    DOI: 10.1093/nar/gkg661
  • Apoptin's functional N- and C-termini independently bind DNA Leliveld SR, Dame RT, Rohn JL, Noteborn MHM, Abrahams JP
    FEBS LETTERS 557, 155 (2003).
    DOI: 10.1016/S0014-5793(03)01465-0
  • Area detectors in structural biology Plaisier JR, Koning RI, Koerten HK, Roon AMvan, Thomassen EAJ, Kuil ME, Hendrix J, Broennimann C, Pannu NS, Abrahams JP
    Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Dectectors and Associated Equipment 509, 274 (2003).
    DOI: 10.1016/S0168-9002(03)01638-3
  • Crystallization and preliminary X-ray analysis of an anti-LewisX Fab fragment with and without its LewisX antigen van Roon AnneMarie M, Pannu Navraj S, Hokke Cornelis H, Deelder Andre M, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 59, 1306 (2003).
    DOI: 10.1107/S0907444903010096
  • Importance of Nuclear Localization of Apoptin for Tumor-specific Induction of Apoptosis Danen-van Oorschot AAAM, Zhang YH, Leliveld SR, Rohn JL, Seelen MCMJ, Bolk MW, van Zon A, Erkeland SJ, Abrahams JP, Mumberg D, Noteborn MHM
    JOURNAL OF BIOLOGICAL CHEMISTRY 278, 27729 (2003).
    DOI: 10.1074/jbc.M303114200
  • Mechanism of Thrombin's Enigmatic Sodium Switch Revealed Abrahams J, Thomassen Ellen AJ
    STRUCTURE 11, 363 (2003).
    DOI: 10.1016/S0969-2126(03)00056-X
  • Prevalent conformations and subunit exchange in the biologically active apoptin protein multimer Leliveld Sirik R, Noteborn Mathieu HM, Abrahams J
    EUROPEAN JOURNAL OF BIOCHEMISTRY 270, 3619 (2003).
    DOI: 10.1046/j.1432-1033.2003.03750.x
  • Recombinant apoptin multimers kill tumor cells but are nontoxic and epitope-shielded in a normal-cell-specific fashion Zhang YH, Leliveld SR, Kooistraa K, Molenaarc C, Rohan JL, Tanker HJ, Abrahams JP, Noteborn MHM
    EXPERIMENTAL CELL RESEARCH 289, 36 (2003).
    DOI: 10.1016/S0014-4827(03)00188-5
  • Structure of ?-Antithrombin and the Effect of Glycosylation on Antithrombin's Heparin Affinity and Activity McCoy Airlie J, Pei X, Skinner R, Abrahams J, Carrell Robin W
    JOURNAL OF MOLECULAR BIOLOGY 326, 823 (2003).
    DOI: 10.1016/S0022-2836(02)01382-7
  • The Functional Integrity of the Serpin Domain of C1-inhibitor Depends on the Unique N-terminal Domain, as Revealed by a Pathological Mutant Bos IGA, Lubbers YTP, Roem D, Abrahams JP, Hack CE, Eldering E
    JOURNAL OF BIOLOGICAL CHEMISTRY 278, 29463 (2003).
    DOI: 10.1074/jbc.M302977200
  • The Structure of the Receptor-binding Domain of the Bacteriophage T4 Short Tail Fibre Reveals a Knitted Trimeric Metal-binding Fold Thomassen E, Gielen G, Schütz M, Schoehn G, Abrahams J, Miller S, van Raaij Mark J
    JOURNAL OF MOLECULAR BIOLOGY 331, 361 (2003).
    DOI: 10.1016/S0022-2836(03)00755-1
  • Visualization by Cryo-electron Microscopy of Genomic RNA that Binds to the Protein Capsid Inside Bacteriophage MS2 Koning R, van den Worm S, Plaisier Jasper R, van Duin J, Abrahams JP, Koerten H
    JOURNAL OF MOLECULAR BIOLOGY 332, 415 (2003).
    DOI: 10.1016/S0022-2836(03)00846-5

2002

  • A novel pH-dependent dimerization motif in ?-lactoglobulin from pig ( Sus scrofa ) Hoedemaeker Flip J, Visschers Ronald W, Alting Arno C, de Kruif Kees G, Kuil Maxim E, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 58, 480 (2002).
    DOI: 10.1107/S0907444902000616
  • Apoptin Induces Tumor-specific Apoptosis as a Globular Multimer Leliveld SR, Zhang YH, Sohn JL, Noteborn MHM, Abrahams JP
    JOURNAL OF BIOLOGICAL CHEMISTRY 278, 9042 (2002).
    DOI: 10.1074/jbc.M210803200
  • Protein nano-crystallogenesis Kuil M, Bodenstaff ERené, Hoedemaeker F, Abrahams J
    ENZYME AND MICROBIAL TECHNOLOGY 30, 262 (2002).
    DOI: 10.1016/S0141-0229(01)00496-3
  • Screening crystallisation conditions using fluorescence correlation spectroscopy Schmauder R, Schmidt T, Abrahams J, Kuil Maxim E
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 58, 1536 (2002).
    DOI: 10.1107/S0907444902014373
  • Structural and Functional Aspects of C1-Inhibitor Bos I, Hack CE, Abrahams JP
    IMMUNOBIOLOGY 205, 518 (2002).
    DOI: 10.1078/0171-2985-00151
  • The prospects of protein nanocrystallography Bodenstaff ERene, Hoedemaeker Flip J, Kuil Maxim E, de Vrind Hans PM, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 58, 1901 (2002).
    DOI: 10.1107/S0907444902016608

2001

  • Matrix methods for solving protein substructures of chlorine and sulfur from anomalous data de Graaff Rudolf AG, Hilge M, van der Plas Jaco L, Abrahams J
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 57, 1857 (2001).
    DOI: 10.1107/S0907444901016535
  • Structure elucidation of ?-mannanase: from the electron-density map to the DNA sequence Hilge M, Perrakis A, Abrahams J, Winterhalter K, Piontek K, Gloor Sergio M
    ACTA CRYSTALLOGRAPHICA SECTION D - BIOLOGICAL CRYSTALLOGRAPHY 57, 37 (2001).
    DOI: 10.1107/S0907444900015547

1999

  • Crystal structure of the C-terminal SH2 domain of the p85? regulatory subunit of phosphoinositide 3-kinase: an SH2 domain mimicking its own substrate Hoedemaeker F, Siegal G, Roe SMark, Driscoll P, Abrahams J
    JOURNAL OF MOLECULAR BIOLOGY 292, 763 (1999).
    DOI: 10.1006/jmbi.1999.3111

1998

  • Implications for function and therapy of a 2.9 å structure of binary-complexed antithrombin Skinner R, Chang W, Jin L, Pei X, Huntington J, Abrahams J, Carrell R, Lomas D
    JOURNAL OF MOLECULAR BIOLOGY 283, 9 (1998).
    DOI: 10.1006/jmbi.1998.2083
  • New developments in phase refinement Abrahams J, De Graaff R
    CURRENT OPINION IN STRUCTURAL BIOLOGY 8, 601 (1998).
    DOI: 10.1016/S0959-440X(98)80151-6
  • Wild-type ?1-antitrypsin is in the canonical inhibitory conformation Elliott P, Abrahams J, Lomas D
    JOURNAL OF MOLECULAR BIOLOGY 275, 419 (1998).
    DOI: 10.1006/jmbi.1997.1458

Former Members

Dr. Tim Gruene

Scientist

+41 56 310 52 97
tim.gruene@psi.ch

Rheinberger,Jan
Ph.D. Student


Schärer,Martin
Ph.D. Student


Wennmacher,Julian
Ph.D. Student

 


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Anita Strittmatter
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Paul Scherrer Institut
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CH-5232 Villigen PSI
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Phone: +41 56 310 20 35
Fax: +41 56 310 21 99
anita.strittmatter@psi.ch

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