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

  1. Author:
    Chen, X.
    Chen, S. M.
    Powell, B. S.
    Court, D. L.
    Ji, X. H.

  2. Author Address

    Ji XH NCI, Biomol Struct Grp, ABL Basic Res Program, Frederick Canc Res & Dev Ctr POB B Ft Detrick, MD 21702 USA NCI, Biomol Struct Grp, ABL Basic Res Program, Frederick Canc Res & Dev Ctr Ft Detrick, MD 21702 USA NCI, Mol Control & Genet Sect, ABL Basic Res Program, Frederick Canc Res & Dev Ctr Ft Detrick, MD 21702 USA Fourth Mil Med Univ, Dept Biochem Xian 710033 Peoples R China
    1. Year: 1999
  2. Journal: Febs Letters
    1. 445
    2. 2-3
    3. Pages: 425-430
  4. Type of Article: Article
  1. Abstract:

    ERA is an essential GTPase widely conserved in bacteria, Homologues of ERA are also present in higher eukaryotic cells. ERA is involved in bacterial cell cycle control at a point preceding cell division. In order to aid the functional investigation of ERA and to facilitate structure-function studies, me have undertaken the X-ray crystallographic analysis of this protein. Here, we report the purification and crystallization procedures and results. The purified ERA exhibits nucleotide-binding activity and GTP-hydrolytic activity. ERA is one of the very few multi-domain GTPases crystallized to date. (C) 1999 Federation of European Biochemical Societies. [References: 21]

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