Dresden 2014 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 5: Protein structure and dynamics I
BP 5.4: Vortrag
Montag, 31. März 2014, 15:45–16:00, ZEU 250
Observation of the size and shape of the initial crystallites involved in crystallisation of the model protein lysozyme — •Raimund J. Heigl1, Andreas Ostermann2, Jörg Stellbrink3, Aurel Radulescu1, Dieter Richter3, and Tobias E. Schrader1 — 1Jülich Centre for Neutron Science JCNS, Forschungszentrum Jülich GmbH, Outstation at MLZ, Lichtenbergstr.1, 85747 Garching, Germany — 2Heinz Maier-Leibnitz Zentrum (MLZ), Lichtenbergstr.1, 85747 Garching, Germany — 3Jülich Centre for Neutron Science JCNS and Institute for Complex Systems ICS, Forschungszentrum Jülich GmbH, 52425 Jülich, Germany
Lysozyme serves as a model protein for the study of protein crystallisation. Yet, the size and shape of the first crystallites leading to the formation of macroscopic crystals is not known. Especially for the method of neutron protein crystallography large crystals need to be grown. Here, good understanding of the evolution of crystal growth would be advantageous. We have found crystallisation conditions of hen egg white lysozyme in D2O which lead to the growth of a fair number of crystals. Preliminary data has been recorded on the small angle neutron scattering (SANS) instrument KWS-2 at the MLZ. It shows a decrease at an intermediate q-range between 0.01 Å−1 and 0.02 Å−1 and an increase at smaller q-values indicating the growth of small crystallites. Dynamic light scattering measurements point to a size distribution of three different hydrodynamic radii. One around 5 nm does not change much with time whereas the middle sized radius rapidly increases.