Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Feb 1;64(Pt 2):94-7. doi: 10.1107/S1744309108000055. Epub 2008 Jan 31.

Abstract

alpha-DsbA1 is one of two DsbA homologues encoded by the Gram-negative alpha-proteobacterium Wolbachia pipientis, an endosymbiont that can behave as a reproductive parasite in insects and as a mutualist in medically important filarial nematodes. The alpha-DsbA1 protein is thought to be important for the folding and secretion of Wolbachia proteins involved in the induction of reproductive distortions. Crystals of native and SeMet alpha-DsbA1 were grown by vapour diffusion and belong to the monoclinic space group C2, with unit-cell parameters a = 71.4, b = 49.5, c = 69.3 A, beta = 107.0 degrees and one molecule in the asymmetric unit (44% solvent content). X-ray data were recorded from native crystals to a resolution of 2.01 A using a copper anode and data from SeMet alpha-DsbA1 crystals were recorded to 2.45 A resolution using a chromium anode.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Polymerase Chain Reaction
  • Protein Disulfide-Isomerases / chemistry*
  • Recombinant Proteins / chemistry
  • Wolbachia / chemistry*

Substances

  • Recombinant Proteins
  • Protein Disulfide-Isomerases