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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 crystallographic studies of the Mycobacterium tuberculosis DNA gyrase ATPase domain

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 25 May 2013

Roué M, Agrawal A, Volker C, Mossakowska D, Mayer C, Bax BD

Link to Pubmed [PMID] – 23722853

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2013 Jun;69(Pt 6):679-82

Mycobacterium tuberculosis DNA gyrase, a nanomachine involved in the regulation of DNA topology, is the only type II topoisomerase present in this organism and hence is the sole target of fluoroquinolones in the treatment of tuberculosis. The ATPase domain provides the energy required for catalysis by ATP hydrolysis. Two constructs corresponding to this 43 kDa domain, Mtb-GyrB47(C1) and Mtb-GyrB47(C2), have been overproduced, purified and crystallized. Diffraction data were collected from three crystal forms. The crystals belonged to space groups P1 and P21 and diffracted to resolutions of 2.9 and 3.3 Å, respectively.

http://www.ncbi.nlm.nih.gov/pubmed/23722853