Premium
Crystallization and preliminary X‐ray diffraction analysis of Gos1p, a yeast SNARE protein
Author(s) -
Cheng Baoyun,
Zhang Yujie,
Guo Gongrui,
Gao Yongxiang
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14011704
Subject(s) - saccharomyces cerevisiae , yeast , endocytic cycle , crystallography , crystallization , membrane , chemistry , lipid bilayer fusion , resolution (logic) , diffraction , golgi apparatus , x ray crystallography , vesicle , biochemistry , receptor , cell , physics , optics , endocytosis , organic chemistry , artificial intelligence , computer science
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 P 2 1 2 1 2 1 , 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 ( V M ) calculations suggest that one molecule is present in the asymmetric unit, corresponding to a solvent content of ∼55%.