title: Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferase.
abstract: The C-terminal domain of adenylyltransferase (ATase) from Escherichia coli has been overexpressed, purified and crystallized in a form suitable for structure analysis. The domain is contained in a fragment that extends from residues 441-945 of the intact ATase.
authors.affiliation: Department of Biochemistry and Molecular Biology, James Cook University, Townsville, Queensland 4811, Australia. yxu@svi.edu.au
authors.forename: Yibin
authors.initials: Y
authors.lastname: Xu
authors.forename: Daying
authors.initials: D
authors.lastname: Wen
authors.forename: Carmen
authors.initials: C
authors.lastname: Brown
authors.forename: Chun-Jung
authors.initials: CJ
authors.lastname: Chen
authors.forename: Paul D
authors.initials: PD
authors.lastname: Carr
authors.forename: David L
authors.initials: DL
authors.lastname: Ollis
authors.forename: Subhash G
authors.initials: SG
authors.lastname: Vasudevan
mesh_terms: D002384:Catalysis; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D008956:Models, Chemical; D009713:Nucleotidyltransferases / Q000737:chemistry*; D010957:Plasmids / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013696:Temperature
chemical_list: D009713:Nucleotidyltransferases; C020658:glutamine-synthetase adenylyltransferase