| Literature DB >> 21301107 |
Andrey Y Kovalevsky1, B Leif Hanson, Sean Seaver, S Zoë Fisher, Marat Mustyakimov, Paul Langan.
Abstract
Room-temperature X-ray and neutron diffraction data were measured from a family 11 endoxylanase holoenzyme (XynII) originating from the filamentous fungus Trichoderma longibrachiatum to 1.55 Å resolution using a home source and to 1.80 Å resolution using the Protein Crystallography Station at LANSCE. Crystals of XynII, which is an important enzyme for biofuel production, were grown at pH 8.5 in order to examine the effect of basic conditions on the protonation-state distribution in the active site and throughout the protein molecule and to provide insights for rational engineering of catalytically improved XynII for industrial applications.Entities:
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Year: 2011 PMID: 21301107 PMCID: PMC3034629 DOI: 10.1107/S174430911005075X
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091