期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 64, 期 -, 页码 636-638出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309108016321
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资金
- Medical Research Council [G0500367] Funding Source: researchfish
- MRC [G0500367] Funding Source: UKRI
- Medical Research Council [G0500367] Funding Source: Medline
Two Bacillus subtilis extracellular endo-1,5-alpha-L-arabinanases, AbnA and Abn2, belonging to glycoside hydrolase family 43 have been identified. The recently characterized Abn2 protein hydrolyzes arabinan and has low identity to other reported 1,5-alpha-L-arabinanases. Abn2 and its selenomethionine (SeMet) derivative have been purified and crystallized. Crystals appeared in two different space groups: P1, with unit-cell parameters a = 51.9, b = 57.6, c = 86.2 angstrom, alpha = 82.3, beta = 87.9, gamma = 63.6 degrees, and P2(1)2(1)2(1), with unit-cell parameters a = 57.9, b = 163.3, c = 202.0 angstrom. X-ray data have been collected for the native and the SeMet derivative to 1.9 and 2.7 angstrom resolution, respectively. An initial model of Abn2 is being built in the SeMet-phased map.
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