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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.

SUBMITTER: Novak WR

PROVIDER: S-EPMC2650460 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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A preliminary neutron diffraction study of gamma-chymotrypsin.

Novak Walter R P WR Moulin Aaron G AG Blakeley Matthew P MP Schlichting Ilme I Petsko Gregory A GA Ringe Dagmar D

Acta crystallographica. Section F, Structural biology and crystallization communications 20090226 Pt 3

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 al ...[more]

PMID: 19255494

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