Catherine L. Tooke

This paper characterizes OXA-57, a class D β-lactamase from Burkholderia pseudomallei, showing its activity against penicillins and cephalosporins, limited carbapenem hydrolysis, and structural insights into its mechanism.

This paper describes a drop on fixed target method for time-resolved serial crystallography, tested with enzymes to improve measurement consistency across facilities.

This study investigates how acyl-enzyme tautomerisation, dynamics, and hydration affect carbapenem antibiotic turnover by OXA-48 β-lactamase using X-ray crystallography and molecular dynamics simulations.

This study uses room-temperature serial crystallography to observe time-dependent ligand dynamics of the β-lactamase CTX-M-15 with avibactam, revealing conformational changes critical for inhibitor reformation.

The paper demonstrates proof of concept for combined droplet on demand serial crystallography and XES experiments at a synchrotron beamline.

This paper investigates how enmetazobactam and tazobactam inhibit GES-1, an ESBL, revealing structural and mechanistic differences in their acyl-enzyme complexes.

This paper compares the potency of nacubactam and avibactam against OXA-48-like β-lactamases, finding that nacubactam is less potent due to electrostatic repulsion with Arg214.

The paper uses dynamical simulations and experiments to identify a distal site in an antibiotic resistance enzyme that modulates activity when mutated.