Open AccessRoom‐temperature ultrahigh‐resolution time‐of‐flight neutron and X‐ray diffraction studies of H/D‐exchanged crambin
Author(s) -
Chen Julian C.H.,
Fisher Zoë,
Kovalevsky Andrey Y.,
Mustyakimov Marat,
Hanson B. Leif,
Zhurov Vladimir V.,
Langan Paul
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111051499
Subject(s) - neutron diffraction , resolution (logic) , crystallography , diffraction , x ray , neutron , materials science , anisotropy , crystal structure , x ray crystallography , chemistry , optics , physics , nuclear physics , artificial intelligence , computer science
The room‐temperature (RT) X‐ray structure of H/D‐exchanged crambin is reported at 0.85 Å resolution. As one of the very few proteins refined with anisotropic atomic displacement parameters at two temperatures, the dynamics of atoms in the RT and 100 K structures are compared. Neutron diffraction data from an H/D‐exchanged crambin crystal collected at the Protein Crystallography Station (PCS) showed diffraction beyond 1.1 Å resolution. This is the highest resolution neutron diffraction reported to date for a protein crystal and will reveal important details of the anisotropic motions of H and D atoms in protein structures.