CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC ANALYSIS OF CHITOSANASE FROM BACILLUS-CIRCULANS MH-K1

被引：7

作者：

SAITO, JI ^{[1
]}

NAGATA, Y ^{[1
]}

ANDO, A ^{[1
]}

KITA, A ^{[1
]}

MIKI, K ^{[1
]}

机构：

[1] CHIBA UNIV,FAC HORT,DIV BIOPROD SCI,MOLEC BIOL LAB,MATSUDO,CHIBA 271,JAPAN

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1995年 / 51卷

关键词：

D O I：

10.1107/S090744499500268X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Chitosanase, an enzyme which hydrolyzes chitosan, isolated from Bacillus circulans MH-K1, was crystallized by a vapor-diffusion procedure at 293 K using ammonium sulfate as a precipitant. Rod-shaped colorless crystals, which grew to 0.05 x 0.15 x 1.2 mm within a week, belong to the orthorhombic system and the space group P222(1) or P2(1)2(1)2 with unit-cell dimensions of a = 43.3, b = 57.7, and c = 128.0 Angstrom. The asymmetric unit is thought to contain one chitosanase molecule (29 024 Da). The crystals diffract X-rays to at least 2.3 Angstrom resolution and are suitable for high-resolution X-ray structure analysis.

引用

页码：856 / 857

页数：2

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