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Time-of-flight neutron diffraction study of bovine [gamma]-chymotrypsin at the Protein Crystallography Station

Journal Article · · Acta Crystallogr. F
The overarching goal of this research project is to determine, for a subset of proteins, exact hydrogen positions using neutron diffraction, thereby improving H-atom placement in proteins so that they may be better used in various computational methods that are critically dependent upon said placement. In order to be considered applicable for neutron diffraction studies, the protein of choice must be amenable to ultrahigh-resolution X-ray crystallography, be able to form large crystals (1 mm{sup 3} or greater) and have a modestly sized unit cell (no dimension longer than 100 {angstrom}). As such, {gamma}-chymotrypsin is a perfect candidate for neutron diffraction. To understand and probe the role of specific active-site residues and hydrogen-bonding patterns in {gamma}-chymotrypsin, neutron diffraction studies were initiated at the Protein Crystallography Station (PCS) at Los Alamos Neutron Science Center (LANSCE). A large single crystal was subjected to H/D exchange prior to data collection. Time-of-flight neutron diffraction data were collected to 2.0 {angstrom} resolution at the PCS with 85% completeness. Here, the first time-of-flight neutron data collection from {gamma}-chymotrypsin is reported.
Research Organization:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Organization:
NIH
OSTI ID:
1030433
Journal Information:
Acta Crystallogr. F, Journal Name: Acta Crystallogr. F Journal Issue: (5) ; 05, 2011 Vol. 67; ISSN 1744-3091
Country of Publication:
United States
Language:
ENGLISH

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