TY - JOUR
T1 - Expression, crystallization and phasing of vacuolar H+-ATPase subunit C (Vma5p) of Saccharomyces cerevisiae
AU - Drory, Omri
AU - Mor, Adi
AU - Frolow, Felix
AU - Nelson, Nathan
PY - 2004/10
Y1 - 2004/10
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=12144270673&partnerID=8YFLogxK
U2 - 10.1107/S0907444904019699
DO - 10.1107/S0907444904019699
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AN - SCOPUS:12144270673
SN - 0907-4449
VL - 60
SP - 1906
EP - 1909
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 10
ER -