Purification, characterization and crystallization of ERA, an essential GTPase from Escherichia coli

ERA is an essential GTPase widely conserved in bacteria, Homologues of ERA are also present in higher eukaryotic cells. ERA is involved in bacterial c ell cycle control at a point preceding cell division. In order to aid the f unctional investigation of ERA and to facilitate structure-function studies , me have undertaken the X-ray crystallographic analysis of this protein. H ere, we report the purification and crystallization procedures and results. The purified ERA exhibits nucleotide-binding activity and GTP-hydrolytic a ctivity. ERA is one of the very few multi-domain GTPases crystallized to da te. (C) 1999 Federation of European Biochemical Societies.