PMID:10944359
| Citation |
Abramson, J, Larsson, G, Byrne, B, Puustinen, A, Garcia-Horsman, A and Iwata, S (2000) Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 56:1076-8 |
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| 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. |
| Links | |
| Keywords |
Crystallization; Crystallography, X-Ray; Cytochromes/chemistry; Cytochromes/isolation & purification; Electron Transport Complex IV/chemistry; Electron Transport Complex IV/isolation & purification; Escherichia coli/enzymology; Escherichia coli Proteins; Models, Molecular; Protein Conformation |
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