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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Crystallization of a proform of aerolysin, a hole-forming toxin from Aeromonas hydrophila
A D Tucker1, M W Parker, D Tsernoglou
1European Molecular Biology Laboratory, Heidelberg, F.R.G.
Journal of Molecular Biology
|April 20, 1990
Abstract:
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.
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