title: A preliminary neutron diffraction study of gamma-chymotrypsin.
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.
authors.affiliation: Departments of Chemistry and Biochemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02454-9110, USA.
authors.forename: Walter R P
authors.initials: WR
authors.lastname: Novak
authors.forename: Aaron G
authors.initials: AG
authors.lastname: Moulin
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Blakeley
authors.forename: Ilme
authors.initials: I
authors.lastname: Schlichting
authors.forename: Gregory A
authors.initials: GA
authors.lastname: Petsko
authors.forename: Dagmar
authors.initials: D
authors.lastname: Ringe
mesh_terms: D002918:Chymotrypsin / Q000737:chemistry*; D003460:Crystallization; D033363:Neutron Diffraction
chemical_list: D002918:Chymotrypsin; C117605:gamma-chymotrypsin