Crystallization and preliminary X-ray diffraction studies of the water-soluble state of the pore-forming toxin sticholysin II from the sea anemone Stichodactyla helianthus

Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1229-31. doi: 10.1107/s090744490200762x. Epub 2002 Jun 20.

Abstract

Sticholysin II (StnII) is a potent cytolytic protein produced by the sea anemone Stichodactyla helianthus. StnII belongs to the actinoporin family, a group of proteins which are characterized by their ability to spontaneously interact with biological membranes. The cytolytic character of these proteins is currently explained in terms of a molecular mechanism involving the formation of transmembrane pores. StnII has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality crystals have unit-cell parameters a = 32.30, b = 119.73, c = 43.42 A, beta = 90.04 degrees and belong to the monoclinic space group P2(1). Diffraction data to a resolution of 1.71 A were collected at synchrotron facilities.

MeSH terms

  • Animals
  • Cnidarian Venoms / chemistry*
  • Crystallography, X-Ray / methods*
  • Hemolysin Proteins / chemistry*
  • Sea Anemones / chemistry*
  • Synchrotrons
  • Temperature
  • Water / chemistry*

Substances

  • Cnidarian Venoms
  • Hemolysin Proteins
  • sticholysin II
  • Water