title: Crystallization and preliminary X-ray crystallographic studies of bovine heart mitochondrial cytochrome bc1 complex.
abstract: Cytochrome bc1 complex (ubiquinol:ferricytochrome c oxidoreductase, EC. 1.10.2.2) from bovine heart mitochondria was crystallized by a batchwise method from protein solution containing sucrose monolaurate using polyethylene glycol-4000 as a precipitant. The red parallelepiped crystals grew to a size of approximately 1 mm x 1 mm x 1 mm. The crystalline protein showed enzymic activity catalyzing electron transfer from ubiquinol-2 to cytochrome c. The subunit composition and absorption spectrum of the crystalline enzyme were identical to those reported previously for the enzyme in solution. The crystal diffracted X-rays to 7.5 A resolution. The diffraction pattern indicated a monoclinic form, space group P2(1), and unit-cell constants of a = 196 A, b = 179 A, c = 253 A and beta = 97 degrees. Most probably four functional units are present in an asymmetric unit.
authors.affiliation: Department of Biology, Faculty of Science, Osaka University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Kubota
authors.forename: M
authors.initials: M
authors.lastname: Kawamoto
authors.forename: K
authors.initials: K
authors.lastname: Fukuyama
authors.forename: K
authors.initials: K
authors.lastname: Shinzawa-Itoh
authors.forename: S
authors.initials: S
authors.lastname: Yoshikawa
authors.forename: H
authors.initials: H
authors.lastname: Matsubara
mesh_terms: D000818:Animals; D002417:Cattle; D014450:Electron Transport Complex III / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D008929:Mitochondria, Heart / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D014450:Electron Transport Complex III