title: Crystallization and preliminary X-ray analysis of the C-terminal domain of δ-COP, a medium-sized subunit of the COPI complex involved in membrane trafficking.
abstract: Coat protein I (COPI) is a protein complex composed of seven subunits that mediates retrograde transport of proteins and lipids from the cis-Golgi network to the endoplasmic reticulum and intra-Golgi membranes. The medium-sized δ subunit of COPI (δ-COP) is a 57 kDa protein with a C-terminal domain (CTD) and an N-terminal longin domain. Here, the δ-COP CTD was successfully cloned, purified and crystallized. Diffraction data were collected from native and selenomethionyl crystals of δ-COP CTD to resolutions of 2.60 and 2.30 Å, respectively. Both crystals belonged to space group P2(1)2(1)2, with similar unit-cell parameters. The native crystals had unit-cell parameters a = 100.23, b = 136.77, c = 44.39 Å.
authors: Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, People's Republic of China.
authors: Kai
authors: K
authors: Deng
authors: Feng
authors: F
authors: Gao
authors: Peng
authors: P
authors: Zheng
authors: Weimin
authors: W
authors: Gong
authors: Zhe
authors: Z
authors: Sun
mesh_terms: D020755:Coat Protein Complex I / Q000737:chemistry*; D020756:Coatomer Protein / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D021122:Protein Subunits / Q000737:chemistry
chemical_list: D020755:Coat Protein Complex I; D020756:Coatomer Protein; D021122:Protein Subunits