| Literature DB >> 19652356 |
Marcus J Edwards1, Ruth H Flatman, Lesley A Mitchenall, Clare E M Stevenson, Anthony Maxwell, David M Lawson.
Abstract
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.Entities:
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Year: 2009 PMID: 19652356 PMCID: PMC2720350 DOI: 10.1107/S1744309109028097
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091