Using rational screening and electron microscopy to optimize the crystallization of succinate:ubiquinone oxidoreductase from Escherichia coli

被引：10

作者：

Horsefield, R

Yankovskaya, V

Törnroth, S

Luna-Chavez, C

Stambouli, E

Barber, J

Byrne, B

Cecchini, G ^{[1
]}

Iwata, S

机构：

[1] Dept Vet Affairs Med Ctr, Div Mol Biol, San Francisco, CA 94121 USA

[2] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AZ, England

[3] Univ Uppsala, BMC, Dept Biochem, S-75123 Uppsala, Sweden

[4] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA

[5] Univ London Imperial Coll Sci Technol & Med, Div Biomed Sci, London SW7 2AZ, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2003年 / 59卷

关键词：

D O I：

10.1107/S0907444903002075

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The membrane-bound respiratory complex II, succinate:ubiquinone oxidoreductase (SQR) from Escherichia coli, has been anaerobically expressed, then purified and crystallized. The initial crystals obtained were small and diffracted poorly. In order to facilitate structure determination, rational screening and sample-quality analysis using electron microscopy was implemented. The crystals of SQR from E. coli belong to the trigonal space group R32, with unit-cell parameters a = b = 138.7, c = 521.9 Angstrom, and diffract to 2.6 Angstrom resolution. The optimization strategy used for obtaining well diffracting SQR crystals is applicable to a wide range of membrane proteins.

引用

页码：600 / 602

页数：3

共 11 条

[1] Phenotypic dichotomy in mitochondrial complex II genetic disorders [J].