Crystallization and preliminary X-ray studies of hORF6, a novel human antioxidant enzyme

Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):436-7. doi: 10.1107/s0907444997011153.

Abstract

HORF6 is a member of the novel antioxidant enzyme family found in humans. A recombinant form of hORF6 expressed and purified from E. coli has been crystallized by the hanging-drop method using various PEG's as precipitating agents. HORF6 crystallizes in two different monoclinic space groups, P21 and C2. The P21 crystals have unit-cell dimensions of a = 47.85, b = 75.17, c = 63.30 A and beta = 110.21 degrees and contain two monomers per asymmetric unit, while the C2 crystals have unit-cell dimensions of a = 165.27, b = 95.44, c = 166.44 A and beta = 128.97 degrees and contain more than six monomers per asymmetric unit. The P21 crystals with the smaller unit cell diffract X-rays better and behave well for the X-ray analysis. A native data set from a single crystal of the P21 space group gas been collected to 2.0 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antioxidants / chemistry*
  • Bacterial Adhesion*
  • Bacterial Proteins / biosynthesis
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Crystallization
  • Escherichia coli
  • Humans
  • Peroxidases / chemistry*
  • Peroxiredoxins
  • Recombinant Proteins / biosynthesis
  • X-Ray Diffraction

Substances

  • Antioxidants
  • Bacterial Proteins
  • Recombinant Proteins
  • Peroxidases
  • Peroxiredoxins