Crystallization and preliminary X-ray analysis of high-alkaline pectate lyase

被引:7
作者
Akita, M
Suzuki, A [1 ]
Kobayashi, T
Ito, S
Yamane, T
机构
[1] Nagoya Univ, Grad Sch Engn, Dept Biotechnol & Biomat Chem, Chikusa Ku, Nagoya, Aichi 4648603, Japan
[2] Kao Corp, Tochigi Res Labs, Haga, Tochigi 3213497, Japan
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷
关键词
D O I
10.1107/S0907444900003334
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Pel-15, a high-alkaline pectate lyase (pectate transeliminase; E.C. 4.2.2.2) from Bacillus sp. strain KSM-P15, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. Two different crystal forms were obtained and preliminary X-ray diffraction data were collected from each crystal form at 100 K. Both forms belong to the orthorhombic space group P2(1)2(1)2(1) and contain one molecule per asymmetric unit. The unit-cell parameters of form I are a = 43.2 (2), b = 60.2 (2), c = 82.2 (2) Angstrom and those of form II are a = 42.9 (1), b = 43.4 (1), c = 105.9 (3) Angstrom. Diffraction data to a resolution of 1.5 Angstrom were collected from form II crystals using a synchrotron-radiation source.
引用
收藏
页码:749 / 750
页数:2
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