Title: Crystallization and preliminary X-ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis
Authors: Vandermarliere, Elien ×
Bourgois, Tine
Van Campenhout, Steven
Strelkov, Sergei
Volckaert, Guido
Delcour, Jan
Courtin, Christophe
Rabijns, Anja #
Issue Date: 1-Jul-2007
Publisher: Wiley-blackwell publishing, inc
Series Title: Acta Crystallographica F, Structural Biology and Crystallization Communications Online vol:63 issue:Pt 8 pages:692-4
Abstract: Arabinoxylan arabinofuranohydrolases (AXH) are alpha-L-arabinofuranosidases (EC that specifically hydrolyse the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl residues from arabinoxylan, hence their name. In this study, the crystallization and preliminary X-ray analysis of the AXH from Bacillus subtilis, a glycoside hydrolase belonging to family 43, is described. Purified recombinant AXH crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 68.7, b = 73.7, c = 106.5 A. X-ray diffraction data were collected to a resolution of 1.55 A.
ISSN: 1744-3091
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biocrystallography
Division of Gene Technology (-)
Centre for Food and Microbial Technology
Faculty of Pharmaceutical Sciences - miscellaneous
× corresponding author
# (joint) last author

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