Crystallization and preliminary X-ray studies of xylanase 10B from Thermotoga maritima

被引：5
|
作者：
Ihsanawati [1 ]
Kumasaka, T [1 ]
Kaneko, T [1 ]
Morokuma, C [1 ]
Nakamura, S [1 ]
Tanaka, N [1 ]
机构：
[1] Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Midori Ku, Kanagawa 2268501, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷
关键词：
D O I：
10.1107/S0907444903015397
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Xylanases catalyze the hydrolysis of the beta-1,4-glycosidic bonds of xylan, which is the second most abundant component of plant cell walls after cellulose. The recombinant xylanase 10B from Thermotoga maritima MSB8 was prepared and crystallized by the sitting-drop vapour-diffusion method using 40 mM zinc acetate, 20 mM MES buffer pH 6.0 and 3% ethanol. Intensity data were collected to 2.5 Angstrom resolution at beamline BL26B2 of SPring-8. Preliminary X-ray analysis showed that the crystal belongs to space group P2(1)2(1)2, with unit-cell parameters a = 77.3, b = 80.6, c = 58.2 Angstrom and one molecule per asymmetric unit.
引用
收藏
页码：1659 / 1661
页数：3
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