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A preliminary neutron diffraction study of γ-chymotrypsin

MPG-Autoren
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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Ringe,  Dagmar
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2650460/pdf/f-65-00317.pdf
(beliebiger Volltext)

http://dx.doi.org/10.1107/S1744309109006630
(beliebiger Volltext)

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Zitation

Novak, W. R. P., Moulin, A. G., Blakeley, M. P., Schlichting, I., Petsko, G. A., & Ringe, D. (2009). A preliminary neutron diffraction study of γ-chymotrypsin. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(3), 317-320. doi:10.1107/S1744309109006630.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0028-79D3-9
Zusammenfassung
The crystal preparation and preliminary neutron diffraction analysis of γ-­chymotrypsin are presented. Large hydrogenated crystals of γ-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 Å 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 γ-­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.