Biophysical Structural Chemistry

Biophysical Structural Chemistry

Research within our group revolves around the atomic structures of large bio-molecules and their complexes.
Autonomous research
within BFSC is focused on fundamental aspects of macromolecular structure determination. Collaborative research with other groups is aimed at understanding macromolecular structure with the biological, functional context. Applied research is spun out into commercial ventures to generate new facilities for fundamental research.

Key publications: 

Prof. dr. J.P. Abrahams
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 Fur Kristallographie, 225 (2-3), 67-76. DOI: 10.1524/zkri.2010.1216

Liu, Z.F., F. Galli, K.G.H. Janssen, L.H. Jiang, H.J. van der Linden, D.C. de Geus, P. Voskamp, M.E. Kuil, R.C.L. Olsthoorn, T.H. Oosterkamp, T. Hankemeier and J.P. Abrahams (2010). Stable Single-Walled Carbon Nanotube-Streptavidin Complex for Biorecognition. Journal of Physical Chemistry C, 114 (10), 4345-4352. DOI: 10.1021/jp911441d

Jiang, L.H., C. Schaffitzel, R. Bingel-Erlenmeyer, N. Ban, P. Korber, R.I. Koning, D.C. de Geus, J.R. Plaisier and J.P. Abrahams (2009). Recycling of Aborted Ribosomal 50S Subunit-Nascent Chain-tRNA Complexes by the Heat Shock Protein Hsp15. Journal of Molecular Biology, 386 (5), 1357-1367. DOI: 10.1016/j.jmb.2008.10.079

Schaffitzel, C., M. Oswald, I. Berger, T. Ishikawa, J.P. Abrahams, H.K. Koerten, R.I. Koning and N. Ban (2006). Structure of the E-coli signal recognition particle bound to a translating ribosome. Nature, 444 (7118), 503-506. DOI: 10.1038/Nature05182

Hilge, M., G. Siegal, G.W. Vuister, P. Guntert, S.M. Gloor and J.P. Abrahams (2003). ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase. Nature Structural Biology, 10 (6), 468-474. DOI: 10.1038/Nsb924

Dr. N.S. Pannu
Skubak, P., W.J. Waterreus and N.S. Pannu (2010). Multivariate phase combination improves automated crystallographic model building. Acta Crystallographica Section D-Biological Crystallography (accepted).

Meulenbroek, E.M., K. Paspaleva, E.A.J. Thomassen, J.P. Abrahams, N. Goosen and N.S. Pannu (2009). Involvement of a carboxylated lysine in UV damage endonuclease. Protein Science, 18 (3), 549-558. DOI: 10.1002/pro.54

Paspaleva, K., E. Thomassen, N.S. Pannu, S. Lwai, G.F. Moolenaar, N. Goosen and J.P. Abrahams (2007). Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease. Structure, 15 (10), 1316-1324. DOI: 10.1016/J.Str.2007.05.010

Skubak, P., G.N. Murshudov and N.S. Pannu (2004). Direct incorporation of experimental phase information in model refinement. Acta Crystallographica Section D-Biological Crystallography, 60 2196-2201. DOI: 10.1107/S0907444904019079

Ness, S.R., R.A. de Graaff, J.P. Abrahams and N.S. Pannu (2004). CRANK: new methods for automated macromolecular crystal structure solution. Structure, 12 (10), 1753-1761. DOI: 10.1016/j.str.2004.07.018