Andrew J. Theobald

TL;DR: This work provides new insights into the mechanism of topoisomerase action and a platform for structure-based drug design of a new class of antibacterial agents against a clinically proven, but conformationally flexible, enzyme class.

TL;DR: The first co-crystal structures of the antibacterial QPT-1 and the anticancer drug etoposide with Staphylococcus aureus DNA gyrase are reported, showing binding at the same sites in the cleaved DNA as the fluoroquinolone moxifloxacin.

TL;DR: A G/T mismatch introduced at the ends of the DNA duplexes facilitated the crystallization of slightly asymmetric complexes of the inherently flexible DNA-cleavage complexes of S. aureus DNA gyrase.

TL;DR: High-purity, full-length, recombinant native enzyme from four Plasmodium species, and thioredoxin substrates from P. falciparum and Rattus norvegicus are produced using a unique, high-throughput, in vitro native substrate assay.

TL;DR: A method for the rapid over-expression and purification of active GST-tagged human topoisomerase IIα using the baculovirus mediated insect cell expression system is reported and validated the enzyme and the high-throughput fluorescence assay as tools for inhibitor identification and selectivity studies.