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Crystallization and preliminary X‐ray crystallographic analysis of subunit F (F

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V‐ATPases are very complex multi‐subunit enzymes which function as proton‐pumping rotary nanomotors. The rotary and coupling subunit F (F1–94) 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 C2221, with unit‐cell parameters a = 47.21, b = 160.26, c = 102.49 Å. The selenomethionyl form of the F1–94 I69M mutant diffracted to a resolution of 2.3 Å and belonged to space group C2221, 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.
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Document Type: Research Article

Affiliations: School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore

Publication date: September 1, 2012

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