Open AccessPreliminary joint X‐ray and neutron protein crystallographic studies of endoxylanase II from the fungus Trichoderma longibrachiatum
Author(s) -
Kovalevsky Andrey Y.,
Hanson B. Leif,
Seaver Sean,
Fisher S. Zoë,
Mustyakimov Marat,
Langan Paul
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911005075x
Subject(s) - protonation , fungus , x ray , neutron diffraction , crystallography , molecule , trichoderma , enzyme , x ray crystallography , active site , chemistry , diffraction , materials science , crystal structure , biology , biochemistry , botany , physics , organic chemistry , optics , ion
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.