Crystallization and preliminary crystallographic studies of CorC, a magnesium-ion transporter

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt 6):681-3. doi: 10.1107/S1744309110012613. Epub 2010 May 26.

Abstract

CorC is a magnesium transporter that is involved in the Mg(2+)-efflux function of the CorA transporter system, an Mg(2+) channel, from Shigella flexneri. Native CorC was purified and crystallized in the native form and in a ligand-free form and diffraction data sets were collected to 2.9 and 3.4 A resolution, respectively. The native CorC crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 64.31, b = 74.44, c = 132.78 A. The ligand-free CorC crystals belonged to space group P3(1)21/P3(2)21, with unit-cell parameters a = b = 71.89, c = 125.96 A. The CorC-ATP complex has also been crystallized and the crystals belonged to space group P2 or P2(1).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism
  • Cation Transport Proteins / chemistry*
  • Cation Transport Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Protein Binding

Substances

  • Cation Transport Proteins
  • Adenosine Triphosphate