| Literature DB >> 2329576 |
A D Tucker1, M W Parker, D Tsernoglou, J T Buckley.
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.Entities:
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Year: 1990 PMID： 2329576 DOI： 10.1016/0022-2836(90)90222-8
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469