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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

Purification, crystallization and preliminary X-ray diffraction experiments on the breakage-reunion domain of the DNA gyrase from Mycobacterium tuberculosis

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 30 Oct 2009

Piton J, Matrat S, Petrella S, Jarlier V, Aubry A, Mayer C

Link to Pubmed [PMID] – 19923746

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2009 Nov;65(Pt 11):1182-6

Mycobacterium tuberculosis DNA gyrase, a nanomachine that is involved in the regulation of DNA topology, is the only type II topoisomerase present in this organism and hence is the sole target for fluoroquinolone action. The breakage-reunion domain of the A subunit plays an essential role in DNA binding during the catalytic cycle. Two constructs of 53 and 57 kDa (termed GA53BK and GA57BK) corresponding to this domain have been overproduced, purified and crystallized. Diffraction data were collected from four crystal forms. The resolution limits ranged from 4.6 to 2.7 angstrom depending on the crystal form. The best diffracting crystals belonged to space group C2, with a biological dimer in the asymmetric unit. This is the first report of the crystallization and preliminary X-ray diffraction analysis of the breakage-reunion domain of DNA gyrase from a species containing one unique type II topoisomerase.

http://www.ncbi.nlm.nih.gov/pubmed/19923746