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. 2009 Mar 1;65(Pt 3):317-20.
doi: 10.1107/S1744309109006630. Epub 2009 Feb 26.

A preliminary neutron diffraction study of gamma-chymotrypsin

Walter R P Novak  1 , Aaron G Moulin, Matthew P Blakeley, Ilme Schlichting, Gregory A Petsko, Dagmar Ringe
Affiliations

A preliminary neutron diffraction study of gamma-chymotrypsin

Walter R P Novak et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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.

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Figures

Figure 1
Figure 1
Photograph of the γ-chymotrypsin crystal used for this neutron diffraction study on the LADI-III beamline at the ILL. The crystal volume is approximately 1.3 mm3.
Figure 2
Figure 2
Neutron Laue diffraction pattern from an 18 h exposure of γ-chymotrypsin using the LADI-III beamline at the ILL.
See this image and copyright information in PMC

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