ArticleActa crystallographica. Section D, Biological crystallography2010
Macromolecular neutron crystallography at the Protein Crystallography Station (PCS).
Article in Acta crystallographica. Section D, Biological crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Perdeuteration, crystallization, data collection and comparison of five neutron diffraction data sets of complexes of human galectin-3C.Acta crystallographica. Section D, Structural biology · 2016Article
- Phase-diagram-guided method for growth of a large crystal of glycoside hydrolase family 45 inverting cellulase suitable for neutron structural analysis.Journal of synchrotron radiation · 2013Article
- Neutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Development and applications of a new neutron single-crystal diffractometer based on a two-dimensional large-area curved position-sensitive detector.Journal of applied crystallography · 2013Article
- Time-of-flight neutron diffraction study of bovine γ-chymotrypsin at the Protein Crystallography Station.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
Corrections and comments
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Authors and funding
6 authors.
Funding
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.
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Registered trials
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