Ontology highlight
ABSTRACT:
SUBMITTER: Ma P
PROVIDER: S-EPMC4600728 | biostudies-literature | 2015 Oct
REPOSITORIES: biostudies-literature
Ma Peixiang P Xue Yi Y Coquelle Nicolas N Haller Jens D JD Yuwen Tairan T Ayala Isabel I Mikhailovskii Oleg O Willbold Dieter D Colletier Jacques-Philippe JP Skrynnikov Nikolai R NR Schanda Paul P
Nature communications 20151005
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 pro ...[more]