Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 65, Issue -, Pages 632-634Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109017230
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Funding
- Japan Society for the Promotion of Science
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beta-L-Arabinopyranosidase from Streptomyces avermitilis NBRC14893 is a monomeric protein consisting of a catalytic domain belonging to glycosyl hydrolase family 27, an unknown domain and a substrate-binding domain belonging to carbohydrate-binding module family 13. The complete enzyme (residues 45-658) has successfully been cloned and homologously expressed in the Streptomyces expression system. beta-L-Arabinopyranosidase was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to 1.6 angstrom resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.2, b = 98.9, c = 181.3 angstrom. The Matthews coefficient was calculated to be 2.38 angstrom(3) Da(-1).
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