DOI > 10.5291/ILL-DATA.8-04-760

This proposal is publicly available since 11/03/2020

Title

Real time study of protein dynamics during a one-step and a two-step crystallization process

Abstract

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.

Experimental Report

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Data Citation

The recommended format for citing this dataset in a research publication is in the following format:

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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Metadata

Experiment Parameters

  • Environment temperature

    295K

Sample Parameters

  • Formula

    • Bovine Beta-Lactoglobulin, ZnCl2, CdCl2, D2O