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Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli

被引：10
作者：
Abramson, J
Larsson, G
Byrne, B
Puustinen, A
Garcia-Horsman, A
Iwata, S
机构：
[1] Uppsala Univ, Dept Biochem, S-75123 Uppsala, Sweden
[2] Univ Helsinki, Dept Med Chem, Helsinki Bioenerget Grp, Helsingin Yilopisto 00014, Finland
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷
关键词：
D O I：
10.1107/S0907444900007605
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Cytochrome bo(3) ubiquinol oxidase has been successfully purified for crystallization. Single crystals of this integral membrane protein diffract X-rays to 3.5 Angstrom resolution and belong to the orthorhombic space group C222(1). From the diffraction data, the unit-cell parameters were determined to be a = 91.3, b = 370.3, c = 232.4 Angstrom. The crystals have a solvent content of 59% and contain two molecules per asymmetric unit. A search model generated from the structures of cytochrome c oxidase from Paracoccus denitrificans and the extrinsic domain of cytochrome bo(3) ubiquinol oxidase from Escherichia coli was used for molecular-replacement studies, resulting in a solution with sensible molecular packing.
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收藏
页码：1076 / 1078
页数：3
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