Macromolecular neutron crystallography at the Protein Crystallography Station (PCS)

✍ Scribed by Kovalevsky, Andrey ;Fisher, Zoe ;Johnson, Hannah ;Mustyakimov, Marat ;Waltman, Mary Jo ;Langan, Paul

• Book ID: 104478577
• Publisher: International Union of Crystallography
• Year: 2010
• Tongue: English
• Weight: 650 KB
• Volume: 66
• Category: Article
• ISSN: 0907-4449
• DOI: 10.1107/s0907444910027198

✦ Synopsis

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.