Open AccessA preliminary neutron diffraction study of γ‐chymotrypsin
Author(s) -
Novak Walter R. P.,
Moulin Aaron G.,
Blakeley Matthew P.,
Schlichting Ilme,
Petsko Gregory A.,
Ringe Dagmar
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109006630
Subject(s) - neutron diffraction , chymotrypsin , materials science , crystallography , resolution (logic) , diffractometer , diffraction , deuterium , neutron , protein crystallization , analytical chemistry (journal) , crystal structure , chemistry , optics , nuclear magnetic resonance , physics , nuclear physics , crystallization , chromatography , enzyme , trypsin , organic chemistry , artificial intelligence , computer science
The crystal preparation and preliminary neutron diffraction analysis of γ‐chymotrypsin are presented. Large hydrogenated crystals of γ‐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 Å 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 γ‐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.