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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):896-9. doi: 10.1107/S1744309111024080. Epub 2011 Jul 19.

Purification and crystallization of yeast glycosylphosphatidylinositol transamidase subunit PIG-S (PIG-S(71-467)).

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1
Bioinformatics Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore. ggrueber@ntu.edu.sg

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.

PMID:
21821889
PMCID:
PMC3151122
DOI:
10.1107/S1744309111024080
[Indexed for MEDLINE]
Free PMC Article
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