Open AccessCrystallization 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
Author(s) -
Edwards Marcus J.,
Flatman Ruth H.,
Mitchenall Lesley A.,
Stevenson Clare E. M.,
Maxwell Anthony,
Lawson David M.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109028097
Subject(s) - dna gyrase , escherichia coli , breakage , crystallization , dna , domain (mathematical analysis) , microbiology and biotechnology , chemistry , genetics , computational biology , biology , crystallography , materials science , gene , organic chemistry , mathematical analysis , mathematics , composite material
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 Å from a single crystal at the synchrotron. DNA gyrase is an essential bacterial enzyme and thus represents an attractive target for drug development.