ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Purification and crystallization of yeast glycosylphosphatidylinositol transamidase subunit PIG-S (PIG-S(71-467)).
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed.
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5 authors.
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Abstract
The transfer of glycosylphosphatidylinositol (GPI) anchors onto eukaryotic proteins is catalyzed by the transamidase complex, which is composed of at least five subunits (PIG-K, PIG-S, PIG-T, PIG-U and GPAA1). Here, the recombinant protein PIG-S(71-467) from Saccharomyces cerevisiae, including residues 71-467 of the entire 534-residue protein, was cloned, expressed and purified to homogeneity. The monodisperse protein was crystallized by the vapour-diffusion method. A diffraction data set was collected to 3.2 Å resolution with 91.6% completeness. The crystals belonged to space group C2, with unit-cell parameters a = 106.72, b = 59.33, c = 124.3 Å, β = 114.19°, and contained two molecules in the asymmetric unit.
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