Silvester Jocelyn A, Dickson Veronica Kane, Runswick Michael J, Leslie Andrew G W, Walker John E
The Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, England.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):530-3. doi: 10.1107/S1744309106015338. Epub 2006 May 5.
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).
牛线粒体ATP合酶外周柄或定子结构域的一个亚复合物已在大肠杆菌中以可溶形式高水平表达。该亚复合物由b亚基的79 - 184位残基、d亚基的1 - 124位残基和整个F6亚基(76个残基)组成。它已通过气相扩散法进行了纯化和结晶。结晶液中存在噻嗯或4 - 甲基吡啶可改善该亚复合物晶体的形态和衍射特性。利用同步辐射源,这些晶体的衍射分辨率达到了2.8埃。它们属于单斜空间群P2(1)。