Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin

被引：9

作者：

Chen, Julian C. -H. ^{[1
]}

Fisher, Zoe ^{[2
]}

Kovalevsky, Andrey Y. ^{[2
]}

Mustyakimov, Marat ^{[2
]}

Hanson, B. Leif ^{[3
]}

Zhurov, Vladimir V. ^{[3
]}

Langan, Paul ^{[3
,4
]}

机构：

[1] Goethe Univ Frankfurt, Inst Biophys Chem, D-60438 Frankfurt, Germany

[2] Los Alamos Natl Lab, Biosci Div, Los Alamos, NM 87545 USA

[3] Univ Toledo, Dept Chem, Toledo, OH 43606 USA

[4] Oak Ridge Natl Lab, Biol & Soft Matter Div, Oak Ridge, TN 37831 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS | 2012年 / 68卷

关键词：

crambin; neutron diffraction; ultrahigh resolution; H; D exchange; DIISOPROPYL FLUOROPHOSPHATASE DFPASE; D-XYLOSE ISOMERASE; PROTEIN CRYSTALLOGRAPHY; SPALLATION NEUTRONS; PROTONATION STATES; ALDOSE REDUCTASE; HYDROGEN; POSITIONS; CRYSTALS; ACCURATE;

D O I：

10.1107/S1744309111051499

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The room-temperature (RT) X-ray structure of H/D-exchanged crambin is reported at 0.85 angstrom 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 angstrom 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.

引用

页码：119 / 123

页数：5

共 4 条

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