| Literature DB >> 17671370 |
Elien Vandermarliere1, Tine M Bourgois, Steven Van Campenhout, Sergei V Strelkov, Guido Volckaert, Jan A Delcour, Christophe M Courtin, Anja Rabijns.
Abstract
Arabinoxylan arabinofuranohydrolases (AXH) are alpha-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 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.Entities:
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Year: 2007 PMID: 17671370 PMCID: PMC2335161 DOI: 10.1107/S1744309107033702
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091