Purification, crystallization and preliminary X-ray analysis of a thermostable direct haemolysin from Grimontia hollisae

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt 2):224-7. doi: 10.1107/S1744309110050219. Epub 2011 Jan 22.

Abstract

Vibrio hollisae, a halophilic species recently reclassified as Grimontia hollisae, is a causative agent of gastroenteritis and septicaemia. One important pathogenic Vibrio factor, thermostable direct haemolysin (TDH), has been purified and crystallized in two crystal forms using the vapour-diffusion method. The crystals belonged to an orthorhombic space group, with unit-cell parameters a = 104.8, b = 112.4, c = 61.3 Å and a = 122.9, b = 123.3, c = 89.8 Å. The crystals contained either four or eight molecules per asymmetric unit, with predicted solvent contents of 49.4 and 46.3% and Matthews coefficients (V(M)) of 2.4 and 2.3 Å(3) Da(-1), respectively. These crystals were suitable for structure determination, which would yield structural details related to the cytotoxicity and oligomeric structure of this pore-forming toxin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Toxins / chemistry
  • Bacterial Toxins / genetics
  • Bacterial Toxins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray / methods
  • Diffusion
  • Hemolysin Proteins / chemistry*
  • Hemolysin Proteins / genetics
  • Hemolysin Proteins / isolation & purification*
  • Molecular Sequence Data
  • Protein Sorting Signals
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Reference Standards
  • Sequence Homology, Amino Acid
  • Synchrotrons
  • Vibrio / chemistry*
  • X-Ray Diffraction

Substances

  • Bacterial Toxins
  • Hemolysin Proteins
  • Protein Sorting Signals
  • Recombinant Proteins
  • thermostable direct hemolysin