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Nat Commun. 2015 Oct 5;6:8361. doi: 10.1038/ncomms9361.

Observing the overall rocking motion of a protein in a crystal.

Author information

1
Université Grenoble Alpes, IBS, F-38044 Grenoble, France.
2
CEA, Institut de Biologie Structurale, F-38044 Grenoble, France.
3
CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France.
4
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.
5
Institut fu¨r Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany.
6
ICS-6: Structural Biochemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.
7
Laboratory of Biomolecular NMR, St. Petersburg State University, St. Petersburg 199034, Russia.

Abstract

The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall 'rocking' motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1-100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments.

PMID:
26436197
PMCID:
PMC4600728
DOI:
10.1038/ncomms9361
[Indexed for MEDLINE]
Free PMC Article

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