Crystallization and preliminary crystallographic studies of Escherichia coli CcmG/DsbE protein

Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1674-5. doi: 10.1107/s0907444903015816. Epub 2003 Aug 19.

Abstract

CcmG/DsbE is a typical thiol/disulfide oxidoreductase, exhibiting a specific reducing activity in a highly oxidizing environment, and is involved in electron transfer during the maturation of c-type cytochromes. Escherichia coli CcmG/DsbE (residues 19-185) has been crystallized using the hanging-drop vapour-diffusion technique. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 35.48, b = 48.52, c = 84.78 A. X-ray data have been collected to 1.9 A resolution.

MeSH terms

  • Crystallization / methods*
  • Crystallography, X-Ray
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / isolation & purification
  • Protein Disulfide Reductase (Glutathione) / chemistry*
  • Protein Disulfide Reductase (Glutathione) / genetics
  • Protein Disulfide Reductase (Glutathione) / isolation & purification

Substances

  • Escherichia coli Proteins
  • Ccmg protein, E coli
  • Protein Disulfide Reductase (Glutathione)