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