Crystallization and preliminary crystallographic analysis of decameric and monomeric forms of C49S mutant thioredoxin-dependent AhpC from Helicobacter pylori

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):394-7. doi: 10.1107/S1744309108008579. Epub 2008 Apr 5.

Abstract

Cys49Ser mutant Helicobacter pylori alkyl hydroperoxide reductase (C49S HpAhpC) was purified under reducing conditions in monomeric and decameric forms. The monomeric form was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.25 A resolution and belonged to space group C2, with unit-cell parameters a = 245.8, b = 140.7, c = 189.5 A, beta = 127 degrees , and contained 20 molecules in the asymmetric unit. A crystal of the decameric form was obtained by the microbatch crystallization method and diffracted to 2.8 A resolution. It belonged to space group C222, with unit-cell parameters a = 257.5, b = 417.5, c = 95.6 A. The structure of the monomeric form of C49S HpAhpC has been solved by the molecular-replacement method.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Crystallography, X-Ray
  • Helicobacter pylori / enzymology*
  • Models, Molecular
  • Molecular Sequence Data
  • Peroxidases / chemistry*
  • Peroxidases / genetics
  • Peroxidases / metabolism
  • Point Mutation
  • Protein Structure, Quaternary*
  • Protein Structure, Tertiary*
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Peroxidases
  • ahpC protein, Helicobacter pylori