Open AccessCrystallization 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
Author(s) -
Deng Kai,
Gao Feng,
Zheng Peng,
Gong Weimin,
Sun Zhe
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112022798
Subject(s) - copi , protein subunit , crystallization , crystallography , domain (mathematical analysis) , terminal (telecommunication) , chemistry , microbiology and biotechnology , materials science , golgi apparatus , biology , biochemistry , engineering , endoplasmic reticulum , secretory pathway , organic chemistry , gene , mathematical analysis , telecommunications , mathematics
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 P 2 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.