Expression, crystallization and phasing of vacuolar H+-ATPase subunit C (Vma5p) of Saccharomyces cerevisiae

Omri Drory, Adi Mor, Felix Frolow*, Nathan Nelson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The expression, crystallization and phasing of subunit C (Vma5p) of the yeast (Saccharomyces cerevisiae) vacuolar proton-translocating ATPase (V-ATPase) is-described. The expressed protein consists of 412 residues: 392 from the reading frame of Vma5p and 20 N-terminal residues originating from the plasmid. Diffraction-quality crystals were obtained using the hanging-drop and sitting-drop vapour-diffusion methods assisted by streak-seeding, with PEG 3350 as precipitant. The crystals formed in hanging drops diffracted to 1.80 Å and belong to space group P432121, with unit-cell parameters a = b = 62.54, c = 327.37 Å, α = β = γ = 90°. The structure was solved using SIRAS with a Lu(O 2C2H3)2 heavy-atom derivative.

Original languageEnglish
Pages (from-to)1906-1909
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number10
DOIs
StatePublished - Oct 2004

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