Crystallization and preliminary X-ray diffraction studies of the hyperthermophilic archaeal sulredoxin having the unique Rieske [2Fe-2S] cluster environment

Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1487-9. doi: 10.1107/S0907444904014295. Epub 2004 Jul 21.

Abstract

The hyperthermophilic archaeal sulredoxin from Sulfolobus tokodaii is a water-soluble high-potential Rieske [2Fe-2S] protein with unique pH-dependent redox properties compared with its mesophilic homologues in cytochrome bc1/b6f complexes. The oxidized recombinant sulredoxin has been crystallized by the hanging-drop vapour-diffusion method using 30%(v/v) polyethylene glycol 400, 0.1 M cadmium chloride and 0.1 M sodium acetate pH 4.6. The crystals diffracted to beyond 2.0 A resolution and belong to the cubic space group F4(1)32, with unit-cell parameter a = 163.00 +/- 0.05 A. The asymmetric unit contains one sulredoxin molecule. Three-wavelength MAD data were collected.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Electron Transport Complex III / chemistry*
  • Electron Transport Complex III / genetics
  • Electron Transport Complex III / metabolism
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / genetics
  • Iron-Sulfur Proteins / metabolism
  • Sulfolobus / chemistry*
  • Sulfolobus / genetics

Substances

  • Archaeal Proteins
  • Iron-Sulfur Proteins
  • Rieske iron-sulfur protein
  • Electron Transport Complex III