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  • Title: Crystallization and preliminary X-ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis.
    Author: Vandermarliere E, Bourgois TM, Van Campenhout S, Strelkov SV, Volckaert G, Delcour JA, Courtin CM, Rabijns A.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2007 Aug 01; 63(Pt 8):692-4. PubMed ID: 17671370.
    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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