Work

A preliminary neutron diffraction study of γ-chymotrypsin

Year: 2009

Type: article

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.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309109006630

Authors: Walter R. P. Novak, Aaron G. Moulin, Matthew P. Blakeley, Ilme Schlichting, Gregory A. Petsko, Dagmar Ringe

Institutions: Brandeis University, Institut Laue-Langevin, Max Planck Society, Max Planck Institute for Medical Research

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

Funders: Alexander von Humboldt-Stiftung, National Institutes of Health, National Institute of General Medical Sciences

Awards: MECHANISMS OF ENZYMIC AND HYDRIDE TRANSFERS, G2699771633, Mechanisms of Enzymic and Hydride Transfers, A Gold-Standard for Hydrogen Sites