Macromolecular neutron crystallography at the Protein Crystallography Station (PCS)

被引:9
作者
Kovalevsky, Andrey [1 ]
Fisher, Zoe [1 ]
Johnson, Hannah [1 ]
Mustyakimov, Marat [1 ]
Waltman, Mary Jo [1 ]
Langan, Paul [1 ]
机构
[1] Los Alamos Natl Lab, Biosci Div, Los Alamos, NM 87545 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2010年 / 66卷
关键词
Protein Crystallography Station; neutron macromolecular crystallography; spallation neutron sources; deuteration; user support; D-XYLOSE ISOMERASE; OF-FLIGHT NEUTRON; X-RAY-DIFFRACTION; DIISOPROPYL FLUOROPHOSPHATASE DFPASE; SURFACE HISTIDYL RESIDUES; NORMAL ADULT HEMOGLOBIN; CARBONIC-ANHYDRASE II; HUMAN DEOXYHEMOGLOBIN; SPALLATION NEUTRONS; PROTONATION STATES;
D O I
10.1107/S0907444910027198
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The Protein Crystallography Station (PCS) at Los Alamos Neutron Science Center is a high-performance beamline that forms the core of a capability for neutron macromolecular structure and function determination. Neutron diffraction is a powerful technique for locating H atoms and can therefore provide unique information about how biological macromolecules function and interact with each other and smaller molecules. Users of the PCS have access to neutron beam time, deuteration facilities, the expression of proteins and the synthesis of substrates with stable isotopes and also support for data reduction and structure analysis. The beamline exploits the pulsed nature of spallation neutrons and a large electronic detector in order to collect wavelength-resolved Laue patterns using all available neutrons in the white beam. The PCS user facility is described and highlights from the user program are presented.
引用
收藏
页码:1206 / 1212
页数:7
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