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Updated: Jul 13, 2026

Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical (Methylation) and Physical (Mass Spectrometry, Nuclear Magnetic Resonance) Techniques
Published on: March 24, 2016
Crystallization and preliminary X-ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis
Elien Vandermarliere1, Tine M Bourgois, Steven Van Campenhout
1Laboratory for Biocrystallography, Katholieke Universiteit Leuven, Herestraat 49, O&N II bus 822, 3000 Leuven, Belgium.
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.
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