Crystallization and preliminary X-ray analysis of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui

被引：16

作者：

Yamada, Y

Saijo, S

Sato, T

Igarashi, N

Usui, H

Fujiwara, T

Tanaka, N

机构：

[1] Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Dept Life Sci, Midori Ku, Yokohama, Kanagawa 2268501, Japan

[2] High Energy Accelerator Res Org, Inst Mat Struct Sci, Tsukuba, Ibaraki 3050801, Japan

[3] Shizuoka Univ, Fac Sci, Dept Biol & Geosci, Shizuoka 4228529, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444901008927

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Catalase-peroxidases are bifunctional enzymes found in many microorganisms. Crystals of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui were obtained using the hanging-drop vapour-diffusion method. The rhombic plate-shaped crystals were grown from purified protein solution using (NH4)(2)SO4 as precipitant at 293 K. The crystal belongs to the monoclinic system, space group C2, and diffracted beyond 2.0 Angstrom resolution.

引用

页码：1157 / 1158

页数：2

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[1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].