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  A preliminary neutron diffraction study of γ-chymotrypsin

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.

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ActaCrystalographicaF_65_317.pdf (Any fulltext), 137KB
 
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 Creators:
Novak, Walter R. P., Author
Moulin, Aaron G., Author
Blakeley, Matthew P., Author
Schlichting, Ilme1, Author           
Petsko, Gregory A., Author
Ringe, Dagmar1, Author           
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: γ-chymotrypsin; neutron diffraction
 Abstract: 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.

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Language(s): eng - English
 Dates: 2008-10-202009-02-232009-02-262009-03-01
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Source Genre: Journal
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Publ. Info: Blackwell Publishing Limited
Pages: - Volume / Issue: 65 (3) Sequence Number: - Start / End Page: 317 - 320 Identifier: ISSN: 1744-3091
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017210_1