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 provid
Neutron protein crystallography in JAERI
β Scribed by I. Tanaka
- Book ID
- 110638025
- Publisher
- Springer-Verlag
- Year
- 2004
- Tongue
- English
- Weight
- 152 KB
- Volume
- 63
- Category
- Article
- ISSN
- 0304-4289
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A description is given of the results of neutron diffraction studies of the structures of four different metal-ion complexes of deuterated D-xylose isomerase. These represent four stages in the progression of the biochemical catalytic action of this enzyme. Analyses of the structural changes observe
Using 'Hydrogen and Hydration in Proteins Data Base' (HHDB) that catalogs all H atom positions in biological macromolecules and in hydration water molecules that have been determined thus far by neutron macromolecular crystallography, methyl group conformation and hydrogen bonds (H.B.) in proteins a