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.
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.
Mancheño
José M
JM
Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Martínez-Ripoll
Martín
M
Gavilanes
José G
JG
Hermoso
Juan A
JA
D000818:Animals; D003064:Cnidarian Venoms / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods*; D006460:Hemolysin Proteins / Q000737:chemistry*; D012615:Sea Anemones / Q000737:chemistry*; D017356:Synchrotrons; D013696:Temperature; D014867:Water / Q000737:chemistry*
D003064:Cnidarian Venoms; D006460:Hemolysin Proteins; C404794:sticholysin II; D014867:Water