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Literature DB >> 16754973

The expression, purification, crystallization and preliminary X-ray analysis of a subcomplex of the peripheral stalk of ATP synthase from bovine mitochondria.

Jocelyn A Silvester¹, Veronica Kane Dickson, Michael J Runswick, Andrew G W Leslie, John E Walker.

Abstract

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 F6 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 A resolution. They belong to the monoclinic space group P2(1).

Entities: Chemical

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Year: 2006 PMID： 16754973 PMCID： PMC2243082 DOI： 10.1107/S1744309106015338

Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091

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Review 10. Scaling and assessment of data quality.

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