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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):829-31. doi: 10.1107/S1744309112022798. Epub 2012 Jun 28.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Coat Protein Complex I / chemistry*
  • Coatomer Protein / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Protein Subunits / chemistry

Substances

  • Coat Protein Complex I
  • Coatomer Protein
  • Protein Subunits