Crystallization of a proform of aerolysin, a hole-forming toxin from Aeromonas hydrophila.
Crystals of proaerolysin, the precursor of the hole-forming toxin from Aeromonas hydrophila, have been obtained. The mature form of this protein binds to a receptor on mammalian cells, aggregates and forms 30 A holes in the membrane. The crystals are tetragonal, space group P4(3)2(1)2, a = b = 104.00 A, c = 222.0 A. They contain a dimer in the asymmetric unit and diffract to a resolution of 2.6 A.
Tucker
A D
AD
European Molecular Biology Laboratory, Heidelberg, F.R.G.
Parker
M W
MW
Tsernoglou
D
D
Buckley
J T
JT
D000333:Aeromonas; D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D052899:Pore Forming Cytotoxic Proteins; D011498:Protein Precursors; D014961:X-Ray Diffraction
D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D052899:Pore Forming Cytotoxic Proteins; D011498:Protein Precursors; C032676:aerolysin