Crystallization and preliminary X-ray analysis of a complex formed between the antibiotic simocyclinone D8 and the DNA breakage-reunion domain of Escherichia coli DNA gyrase.
Crystals of a complex formed between the 59 kDa N-terminal fragment of the Escherichia coli DNA gyrase A subunit (also known as the breakage-reunion domain) and the antibiotic simocyclinone D8 were grown by vapour diffusion. The complex crystallized with I-centred orthorhombic symmetry and X-ray data were recorded to a resolution of 2.75 A from a single crystal at the synchrotron. DNA gyrase is an essential bacterial enzyme and thus represents an attractive target for drug development.
Edwards
Marcus J
MJ
Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, England.
Flatman
Ruth H
RH
Mitchenall
Lesley A
LA
Stevenson
Clare E M
CE
Maxwell
Anthony
A
Lawson
David M
DM
D003374:Coumarins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D004249:DNA Damage; D027081:DNA Gyrase / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D006027:Glycosides / Q000737:chemistry; D008968:Molecular Conformation
D003374:Coumarins; D006027:Glycosides; C416814:simocyclinone D8; D027081:DNA Gyrase