Basak S, et al. (2012) Crystallization and preliminary X-ray crystallographic analysis of subunit F (F(1-94)), an essential coupling subunit of the eukaryotic V(1)V(O)-ATPase from Saccharomyces cerevisiae. Acta Crystallogr Sect F Struct Biol Cryst Commun 68(Pt 9):1055-9
Abstract: V-ATPases are very complex multi-subunit enzymes which function as proton-pumping rotary nanomotors. The rotary and coupling subunit F (F(1-94)) was crystallized by the hanging-drop vapour-diffusion method. The native crystals diffracted to a resolution of 2.64 A and belonged to space group C222(1), with unit-cell parameters a = 47.21, b = 160.26, c = 102.49 A. The selenomethionyl form of the F(1-94) I69M mutant diffracted to a resolution of 2.3 A and belonged to space group C222(1), with unit-cell parameters a = 47.22, b = 160.83, c = 102.74 A. Initial phasing and model building suggested the presence of four molecules in the asymmetric unit.
|Status: Published||Type: Journal Article||PubMed ID: 22949193|
Topics addressed in this paper
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|Protein Physical Properties|
|Protein/Nucleic Acid Structure|