Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei

被引:4
作者
Hakulinen, N
Tenkanen, M
Rouvinen, J
机构
[1] Univ Joensuu, Dept Chem, FIN-80101 Joensuu, Finland
[2] VTT Biotechnol & Food Res, Espoo 02044, Finland
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1998年 / 54卷
关键词
D O I
10.1107/S0907444997012213
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Acetyl xylan esterase is involved in the biodegradation of hemicellulose. It cleaves O-acetyl groups from xylan, which is the most abundant hemicellulose in nature. The catalytic core of acetyl xylan esterase from T. reesei has been crystallized and X-ray diffraction data at 2.3 Angstrom collected. The crystal belongs to the triclinic space group P1 with unit-cell parameters a = 50.3, b = 62.1, c = 40.0 Angstrom, alpha = 110.1, beta = 113.6 and gamma = 97.9 degrees. The asymmetric unit contains two molecules.
引用
收藏
页码:430 / 432
页数:3
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