PMID:8865345

Citation	Peat, TS, Frank, EG, Woodgate, R and Hendrickson, WA (1996) Production and crystallization of a selenomethionyl variant of UmuD', an Escherichia coli SOS response protein. Proteins 25:506-9
Abstract	Crystals of both native and mutant Escherichia coli UmuD' protein were obtained using the hanging drop method. Soaking the native crystals in solutions of heavy metal ions failed to produce good isomorphous derivatives, and selenomethionine substituted wild-type protein did not crystallize under conditions that gave native crystals. Site-directed mutagenesis was used to change the penultimate residue, a methionine amino acid, to either a valine or a threonine amino acid. Crystals were subsequently obtained from these mutant proteins with and without selenomethionine incorporation. Crystals of the native, the mutant, and the selenomethionine incorporated protein were all similar, crystallizing in the P4(1)2(1)2 space group.
Links	PubMed Online version:10.1002/prot.10
Keywords	Amino Acid Sequence; Bacterial Proteins/biosynthesis; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Crystallography, X-Ray; DNA-Directed DNA Polymerase; Escherichia coli Proteins; Molecular Sequence Data; Mutagenesis; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Sequence Homology, Amino Acid
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