Crystallization of a proform of aerolysin, a hole-forming toxin from Aeromonas hydrophila |
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Authors: | A D Tucker M W Parker D Tsernoglou J T Buckley |
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Affiliation: | European Molecular Biology Laboratory, Heidelberg, F.R.G. |
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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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