Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin

Susanne C. Feil, Jamie Rossjohn, Kyle Rohde, Rodney K. Tweten, Michael W. Parker

Research output: Contribution to journalArticleResearchpeer-review

17 Citations (Scopus)


We present the first reported crystallization of a member of the thiol-activated family of protein toxins. Perfringolysin 0, a virulence factor of Clostridium perfringens, has been crystallized in two different forms by the hanging drop vapor diffusion method. In one form the toxin crystallizes with PEG 20000 in the orthorhombic space group C2221 with cell dimensions of a = 47.8 Å, b = 182.0 Å and c 175.5 Å and the crystals diffract to beyond 2.5 Å resolution. In the second form the toxin crystallizes in a large variety of organic solvents including malt whisky. This crystal form belongs to the orthorhombic space group P2221 with unit cell dimensions a = 47.1 Å, b = 166.1 Å and c = 214.0 Å and with diffraction observed to 2.4 Å resolution.

Original languageEnglish
Pages (from-to)290-292
Number of pages3
JournalFEBS Letters
Issue number2-3
Publication statusPublished - 18 Nov 1996
Externally publishedYes


  • Crystallization
  • Perfringolysin 0
  • Pore-forming toxin
  • Thiol-activated cytolysin
  • X-ray diffraction

Cite this