Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli.
Cytochrome bo(3) ubiquinol oxidase has been successfully purified for crystallization. Single crystals of this integral membrane protein diffract X-rays to 3.5 A 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 A. 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.
Abramson
J
J
Uppsala University Department of Biochemistry, BMC BOX 576, S-75123 Uppsala, Sweden.
Larsson
G
G
Byrne
B
B
Puustinen
A
A
Garcia-Horsman
A
A
Iwata
S
S
D003460:Crystallization; D018360:Crystallography, X-Ray; D003573:Cytochrome b Group; D003580:Cytochromes / Q000737:chemistry* / Q000302:isolation & purification*; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000302:isolation & purification*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D011487:Protein Conformation
D003573:Cytochrome b Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; C083850:cytochrome bo3, E coli; C038862:cytochrome o oxidase; D003576:Electron Transport Complex IV