Real time study of protein dynamics during a non-classical crystallization process

DOI

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 a suitable crystallizing systems by QENS at IN11 may provide new extremely useful information, thus potentially significantly improving the general physical picture. This proposal continues the IN16B and IN11 work.

Identifier
DOI https://doi.org/10.5291/ILL-DATA.8-04-766
Metadata Access https://data.ill.fr/openaire/oai?verb=GetRecord&metadataPrefix=oai_datacite&identifier=10.5291/ILL-DATA.8-04-766
Provenance
Creator Sohmen, Benedikt; Beck, Christian; Zhang, Fajun; Roosen-Runge, Felix; Schreiber, Frank; Grimaldo, Marco; Feustel, Michal; Czakkel, Orsolya; Seydel, Tilo
Publisher Institut Laue-Langevin
Publication Year 2017
Rights OpenAccess; info:eu-repo/semantics/openAccess
OpenAccess true
Representation
Resource Type Dataset
Size 646 MB
Version 1
Discipline Particles, Nuclei and Fields