| Literature DB >> 19255494 |
Walter R P Novak1, Aaron G Moulin, Matthew P Blakeley, Ilme Schlichting, Gregory A Petsko, Dagmar Ringe.
Abstract
The crystal preparation and preliminary neutron diffraction analysis of gamma-chymotrypsin are presented. Large hydrogenated crystals of gamma-chymotrypsin were exchanged into deuterated buffer via vapor diffusion in a capillary and neutron Laue diffraction data were collected from the resulting crystal to 2.0 A resolution on the LADI-III diffractometer at the Institut Laue-Langevin (ILL) at room temperature. The neutron structure of a well studied protein such as gamma-chymotrypsin, which is also amenable to ultrahigh-resolution X-ray crystallography, represents the first step in developing a model system for the study of H atoms in protein crystals.Entities:
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Year: 2009 PMID: 19255494 PMCID: PMC2650460 DOI: 10.1107/S1744309109006630
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091