Our main research projects focus on structural and functional studies of M. tuberculosis DNA gyrase and aim to understand the structural dynamics of DNA recognition by DNA gyrase and the quinolone resistance mechanisms in the treatment of tuberculosis. We have determined the crystal structures of the four functional M. tuberculosis DNA gyrase domains, the breakage-reunion, the Toprim, the CTD and the ATPase domains. Current studies address fundamental questions concerning how type II topoisomerases are working, notably by studying the full-length M. tuberculosis DNA gyrase using X-ray crystallography, SAXS and cryo-EM, but also in depth questions concerning specificities of M. tuberculosis DNA gyrase. We extend these studies to other type II topoisomerases, e.g. P. falciparum DNA gyrase, archaeal gyrases, archaeal and eukaryotic topoisomerases VI and the very recently discovered topoisomerases VIII (Gadelle D, Krupovic M, Raymann K, Mayer C, Forterre P. DNA topoisomerase VIII: a novel subfamily of type IIB topoisomerases encoded by free or integrated plasmids in Archaea and Bacteria. Nucleic Acids Res. 2014 Jul;42(13):8578-91. doi: 10.1093/nar/gku568. Epub 2014 Jul 2. PubMed PMID: 24990376).