Crystallization and preliminary X-ray diffraction analysis of Gos1p, a yeast SNARE protein

Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):967-9. doi: 10.1107/S2053230X14011704. Epub 2014 Jun 19.

Abstract

The Gos1 protein (Golgi SNAP receptor complex member 1) is involved in the SNARE complex, which is the core machinery that drives membrane fusion between cargo-carrying vesicles and their target membranes in the secretory and endocytic pathways in yeast. Truncated versions of the Gos1 protein from Saccharomyces cerevisiae were cloned, expressed, purified and crystallized. The crystal belonged to space group P2₁2₁2₁, with unit-cell parameters a=39.67, b=43.58, c=81.94 Å, α=β=γ=90°. An X-ray diffraction data set was collected at 100 K to 1.63 Å resolution. Matthews coefficient (VM) calculations suggest that one molecule is present in the asymmetric unit, corresponding to a solvent content of ∼55%.

Keywords: Gos1 protein; SNARE complex; Saccharomyces cerevisiae; membrane fusion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Transport
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • SNARE Proteins / chemistry*
  • SNARE Proteins / genetics
  • SNARE Proteins / metabolism
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism

Substances

  • GOS1 protein, S cerevisiae
  • Recombinant Proteins
  • SNARE Proteins
  • Saccharomyces cerevisiae Proteins