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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 18: Crystallization, Nucleation and Self-Assembly II (joint session CPP/BP)
CPP 18.1: Vortrag
Dienstag, 2. April 2019, 09:30–09:45, H14
Investigation of the Short-Time Diffusive Dynamics During Salt-Induced Protein Crystallization Using Neutron Spectroscopy — •Christian Beck1,2, Marco Grimaldo1, Felix Roosen-Runge3, Fajun Zhang2, Frank Schreiber2, and Tilo Seydel1 — 1Institut Laue Langevin, Grenoble, France — 2University of Tübingen, Germany — 3Lund University, Lund, Sweden
Protein crystals are needed to obtain high-resolution protein structures, and therefore understanding different processes/pathways leading to their formation is of fundamental biophysical and medical interest. Previous studies investigating the kinetics of crystallization in situ using static methods (SAXS and microscopy) provided evidence for non-classical crystallization pathways in the presence of multivalent salts [1,2]. Using dissolved β-lactoglobulin proteins as a model system, we studied the ZnCl2-induced crystallization. Here, we employ quasi-elastic neutron backscattering (NBS) and neutron spin-echo (NSE) spectroscopy to access the kinetics of the nanosecond diffusive dynamics of proteins during crystallization on a nanometer length scale. NBS provides information on the changes of the center-of-mass diffusion, internal diffusive dynamics and on the fraction of immobile proteins associated with the crystals. Accessing coherent scattering with NSE, we probe different scattering vectors q to disentangle the different diffusive contributions of proteins in crystals or aggregates, and in the liquid phase, respectively.
[1] A. Sauter et al. ACS Cryst. Growth Des. 14 (2014) 6357
[2] A. Sauter et al. Faraday Discuss. 179 (2015) 41