Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferase.
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.
Xu
Yibin
Y
Department of Biochemistry and Molecular Biology, James Cook University, Townsville, Queensland 4811, Australia. yxu@svi.edu.au
Wen
Daying
D
Brown
Carmen
C
Chen
Chun-Jung
CJ
Carr
Paul D
PD
Ollis
David L
DL
Vasudevan
Subhash G
SG
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
D009713:Nucleotidyltransferases; C020658:glutamine-synthetase adenylyltransferase