The expression, purification, crystallization and preliminary X-ray analysis of a subcomplex of the peripheral stalk of ATP synthase from bovine mitochondria.
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).
Silvester
Jocelyn A
JA
The Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, England.
Dickson
Veronica Kane
VK
Runswick
Michael J
MJ
Leslie
Andrew G W
AG
Walker
John E
JE
D000818:Animals; D002417:Cattle; D003460:Crystallization; D024101:Mitochondrial Proteins / Q000737:chemistry; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry*; D046912:Multiprotein Complexes / Q000737:chemistry; D014961:X-Ray Diffraction
D024101:Mitochondrial Proteins; D046912:Multiprotein Complexes; D025261:Mitochondrial Proton-Translocating ATPases