The expression and crystallization of the VMA13p subunit of the vacuolar proton-translocating ATPase (V-ATPase) of Saccharomyces cerevisiae is described. This 478 amino-acid subunit is essential for activity but not for the assembly of this multisubunit complex. The protein has been recombinantly overexpressed in Escherichia coli and purified. Diffraction-quality crystals have been obtained using the hanging-drop vapor-diffusion method with ammonium sulfate as precipitant. Several different crystal forms were obtained. The most suitable crystal form for crystallographic characterization belongs to space group P3(1)21 or its enantiomorph, with unit-cell parameters a = b = 118.8, c = 119.3 A. Using an in-house X-ray source, the crystals diffract to about 3.5 A resolution under rapidly frozen conditions.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|