Unknown

Dataset Information

0

Macromolecular neutron crystallography at the Protein Crystallography Station (PCS).


ABSTRACT: 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.

SUBMITTER: Kovalevsky A 

PROVIDER: S-EPMC2967422 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Macromolecular neutron crystallography at the Protein Crystallography Station (PCS).

Kovalevsky Andrey A   Fisher Zoe Z   Johnson Hannah H   Mustyakimov Marat M   Waltman Mary Jo MJ   Langan Paul P  

Acta crystallographica. Section D, Biological crystallography 20101020 Pt 11


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 exp  ...[more]

Similar Datasets

| S-EPMC5331467 | biostudies-literature
| S-EPMC4388167 | biostudies-literature
| S-EPMC4051545 | biostudies-literature
| S-EPMC3083928 | biostudies-literature
| S-EPMC7571246 | biostudies-literature
| S-EPMC2967424 | biostudies-literature
| S-EPMC2394825 | biostudies-literature
| S-EPMC3795564 | biostudies-literature
| S-EPMC2586829 | biostudies-literature
| S-EPMC4791750 | biostudies-literature