Real time study of protein dynamics during a one-step and a two-step crystallization process
Protein crystallization is of great interest due to its crucial role for the determination of protein structures, as well as in other fields such as drug engineering by pharmaceutical industries [J. Gunton et al. Protein Condensation: Kinetic Pathways to Crystallization and Disease. CUP, (2007)]. Despite its importance, a fundamental understanding of the mechanisms underlying such a process is still missing. Recently, both experimental [F. Zhang et al. Journal of Applied Crystallography 44, (2011); A.Sauter et al., J.Am.Chem.Soc. 137, 1485 (2015)] and theoretical [P. G. Vekilov, Nanoscale 2, (2010)] studies have shown that, under certain conditions, crystallization follows a multi-step mechanism, rather than the classical nucleation pathway. In order to gain a better understanding of such processes, an in situ study of the dynamics of two suitable crystallizing systems by QENS at IN16B and IN11 may provide new extremely useful information, thus potentially significantly improving the general physical picture. This proposal continues the IN16B work and adds IN11 to measure on and off the correlation peak found in SANS.
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GRIMALDO Marco; BECK Christian; CZAKKEL Orsolya; FEUSTEL Michal; ROOSEN RUNGE Felix; SAUTER Andrea; Frank Schreiber; SEYDEL Tilo and ZHANG Fajun. (2015). Real time study of protein dynamics during a one-step and a two-step crystallization process. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-760
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