Open AccessCrystallization 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
Author(s) -
Basak Sandip,
Balakrishna Asha Manikkoth,
Manimekalai Malathy Sony Subramanian,
Grüber Gerhard
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112032526
Subject(s) - protein subunit , crystallography , crystallization , resolution (logic) , atpase , diffraction , coupling (piping) , x ray crystallography , molecule , materials science , chemistry , enzyme , physics , optics , biochemistry , organic chemistry , artificial intelligence , computer science , metallurgy , gene
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 C 222 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 C 222 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.