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Crystallization and preliminary X‐ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis

Crystallization and preliminary X‐ray analysis of an arabinoxylan arabinofuranohydrolase from... 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 P212121, 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary X‐ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis

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References (14)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309107033702
pmid
17671370
Publisher site
See Article on Publisher Site

Abstract

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 P212121, 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.

Journal

Acta Crystallographica Section FWiley

Published: Aug 1, 2007

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