title: Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli.
abstract: 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.
authors.affiliation: Uppsala University Department of Biochemistry, BMC BOX 576, S-75123 Uppsala, Sweden.
authors.forename: J
authors.initials: J
authors.lastname: Abramson
authors.forename: G
authors.initials: G
authors.lastname: Larsson
authors.forename: B
authors.initials: B
authors.lastname: Byrne
authors.forename: A
authors.initials: A
authors.lastname: Puustinen
authors.forename: A
authors.initials: A
authors.lastname: Garcia-Horsman
authors.forename: S
authors.initials: S
authors.lastname: Iwata
mesh_terms: 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
chemical_list: D003573:Cytochrome b Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; C083850:cytochrome bo3, E coli; C038862:cytochrome o oxidase; D003576:Electron Transport Complex IV