Time-of-flight neutron diffraction study of bovine γ-chymotrypsin at the protein crystallography station

Louis M. Lazar, S. Zoe Fisher, Aaron G. Moulin, Andrey Kovalevsky, Walter R.P. Novak, Paul Langan, Gregory A. Petsko, Dagmar Ringe

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The overarching goal of this research project is to determine, for a subset of proteins, exact hydrogen positions using neutron diffraction, thereby improving H-atom placement in proteins so that they may be better used in various computational methods that are critically dependent upon said placement. In order to be considered applicable for neutron diffraction studies, the protein of choice must be amenable to ultrahigh-resolution X-ray crystallography, be able to form large crystals (1 mm3 or greater) and have a modestly sized unit cell (no dimension longer than 100 Å). As such, γ-chymotrypsin is a perfect candidate for neutron diffraction. To understand and probe the role of specific active-site residues and hydrogen-bonding patterns in γ-chymotrypsin, neutron diffraction studies were initiated at the Protein Crystallography Station (PCS) at Los Alamos Neutron Science Center (LANSCE). A large single crystal was subjected to H/D exchange prior to data collection. Time-of-flight neutron diffraction data were collected to 2.0 Å resolution at the PCS with ∼85% completeness. Here, the first time-of-flight neutron data collection from γ-chymotrypsin is reported.

Original languageEnglish
Pages (from-to)587-590
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number5
DOIs
StatePublished - May 2011
Externally publishedYes

Keywords

  • -chymotrypsin
  • neutron diffraction

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