title: 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.
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 Å and belonged to space group C222(1), with unit-cell parameters a = 47.21, b = 160.26, c = 102.49 Å. The selenomethionyl form of the F(1-94) I69M mutant diffracted to a resolution of 2.3 Å and belonged to space group C222(1), with unit-cell parameters a = 47.22, b = 160.83, c = 102.74 Å. Initial phasing and model building suggested the presence of four molecules in the asymmetric unit.
authors.affiliation: School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.
authors.forename: Sandip
authors.initials: S
authors.lastname: Basak
authors.forename: Asha Manikkoth
authors.initials: AM
authors.lastname: Balakrishna
authors.forename: Malathy Sony Subramanian
authors.initials: MS
authors.lastname: Manimekalai
authors.forename: Gerhard
authors.initials: G
authors.lastname: Grüber
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry*
chemical_list: D029701:Saccharomyces cerevisiae Proteins; C089600:VMA7 protein, S cerevisiae; D025262:Vacuolar Proton-Translocating ATPases