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

Authors
  • Cheng, Baoyun
  • Zhang, Yujie
  • Guo, Gongrui
  • Gao, Yongxiang
Type
Published Article
Journal
Acta crystallographica. Section F, Structural biology communications
Publication Date
Jul 01, 2014
Volume
70
Issue
Pt 7
Pages
967–969
Identifiers
DOI: 10.1107/S2053230X14011704
PMID: 25005100
Source
Medline
Keywords
License
Unknown

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%.

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