The expression, purification, crystallization and preliminary X-ray analysis of a subcomplex of the peripheral stalk of ATP synthase from bovine mitochondria
- The Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY (United Kingdom)
- The Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH (United Kingdom)
A recombinant subcomplex of the peripheral stalk or stator domain of the ATP synthase from bovine mitochondria has been crystallized and a native data set has been collected to 2.8 Å resolution. A subcomplex of the peripheral stalk or stator domain of the ATP synthase from bovine mitochondria has been expressed to high levels in a soluble form in Escherichia coli. The subcomplex consists of residues 79–184 of subunit b, residues 1–124 of subunit d and the entire F{sub 6} subunit (76 residues). It has been purified and crystallized by vapour diffusion. The morphology and diffraction properties of the crystals of the subcomplex were improved by the presence of thioxane or 4-methylpyridine in the crystallization liquor. With a synchrotron-radiation source, these crystals diffracted to 2.8 Å resolution. They belong to the monoclinic space group P2{sub 1}.
- OSTI ID:
- 22360219
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 6; Other Information: PMCID: PMC2243082; PMID: 16754973; PUBLISHER-ID: bw5146; OAI: oai:pubmedcentral.nih.gov:2243082; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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