In situ real-time study of the diffusive dynamic arrest of proteins during crystallization
Protein crystallization plays an important role in structural biology and medicine. Different crystallization pathways have been identified, but a general understanding of the fundamental processes is still missing. Different pathways can be addressed by choosing different salts and changing its concentration. Investigating the dynamics of the proteins may offer new insights playing a key-role in the understanding of the crystallization. In already allocated time, based on previous successful results, we will investigate the dynamics during the crystallization process using the unique inelastic fixed window scans on IN16B to significantly increase existing data for a comprehensive and reliable picture, as well as the structural evolution using SANS on D11. Here, we propose a complementary spin-echo experiment on the crystallizing samples to monitor the dynamic changes on and besides the Bragg and monomer-monomer peaks in-situ. This experiment can be done on IN11, but would be ideally suited as an early demonstration experiment on WASP, by observing the evolution on the Bragg and monomer-monomer peaks as well as off these peaks simultaneously, using the same samples as on IN16B.
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BECK Christian; BAEUERLE Famke; CZAKKEL Orsolya; GIRELLI Anita; GRIMALDO Marco; MAIER Ralph; MATSARSKAIA Olga; ROOSEN RUNGE Felix; Frank Schreiber; SEYDEL Tilo and ZHANG Fajun. (2020). In situ real-time study of the diffusive dynamic arrest of proteins during crystallization. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-862
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