title: Crystallographic phases through genetic engineering: experiences with colicin A.
abstract: Colicins are antibiotic proteins that kill sensitive Escherichia coli cells. The structure of the pore-forming fragment of colicin A has been solved to 2.5 A resolution using the techniques of X-ray crystallography and genetic engineering. Site-directed mutagenesis was used to construct a number of cysteine-containing mutant proteins, one of which yielded an excellent mercurial derivative. Our experiences suggest strategies for obtaining useful heavy-atom derivatives for protein crystallography using genetic engineering techniques.
authors.affiliation: European Molecular Biology Laboratory, Heidelberg, FRG.
authors.forename: A D
authors.initials: AD
authors.lastname: Tucker
authors.forename: D
authors.initials: D
authors.lastname: Baty
authors.forename: M W
authors.initials: MW
authors.lastname: Parker
authors.forename: F
authors.initials: F
authors.lastname: Pattus
authors.forename: C
authors.initials: C
authors.lastname: Lazdunski
authors.forename: D
authors.initials: D
authors.lastname: Tsernoglou
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification*; D001483:Base Sequence; D003087:Colicins; D003461:Crystallography; D004926:Escherichia coli; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015202:Protein Engineering
chemical_list: D001426:Bacterial Proteins; D003087:Colicins; C007104:colicin immunity proteins