ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Cytochrome bo3 ubiquinol oxidase has been successfully purified for crystallization. Single crystals of this integral membrane protein diffract X-rays to 3.5 Å resolution and belong to the orthorhombic space group C2221. From the diffraction data, the unit-cell parameters were determined to be a = 91.3, b = 370.3, c = 232.4 Å. 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 bo3 ubiquinol oxidase from Escherichia coli was used for molecular-replacement studies, resulting in a solution with sensible molecular packing.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444900007605