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The complex between the ribonuclease domain of the ribosome-inactivating colicin E3 and its protein inhibitor, the cognate immunity Im3, has been crystallized and preliminary X-ray characterization has been performed. Single crystals of the 1:1 complex were grown from hanging-drop vapour-diffusion experiments using 2-propanol as a precipitant. The space group is P3(1)21 or P3(2)21, with unit-cell parameters a = b = 93.7, c = 76.2 A. When cryocooled, these crystals diffract to a resolution of 2.4 A. A search for suitable conventional heavy-atom derivatives was unsuccessful and so Im3 mutants containing engineered cysteine or methionine residues have been produced for mercury soaks and selenomethionine-labelling experiments, respectively.


Journal article


Acta Crystallogr D Biol Crystallogr

Publication Date





1630 - 1633


Amino Acid Substitution, Bacterial Proteins, Binding Sites, Colicins, Crystallization, Crystallography, X-Ray, Escherichia coli, Escherichia coli Proteins, Mercury, Methionine, Mutagenesis, Site-Directed, Protein Conformation, Ribonucleases, Selenomethionine, Serine