Open AccessCrystallization and preliminary X‐ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis
Author(s) -
Vandermarliere Elien,
Bourgois Tine M.,
Van Campenhout Steven,
Strelkov Sergei V.,
Volckaert Guido,
Delcour Jan A.,
Courtin Christophe M.,
Rabijns Anja
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107033702
Subject(s) - arabinoxylan , crystallization , bacillus subtilis , orthorhombic crystal system , chemistry , glycosidic bond , resolution (logic) , crystallography , glycoside hydrolase , hydrolysis , crystal structure , organic chemistry , enzyme , biology , genetics , bacteria , artificial intelligence , computer science
Arabinoxylan arabinofuranohydrolases (AXH) are α‐ l ‐arabinofuranosidases (EC 3.2.1.55) 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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 68.7, b = 73.7, c = 106.5 Å. X‐ray diffraction data were collected to a resolution of 1.55 Å.