Philip Hinchliffe

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 designs de novo flavoproteins with controlled excited state dynamics using computational methods and experimental validation.

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.

The paper identifies and characterizes intramolecular isopeptide bonds in protein domains across organisms, revealing their structural and functional significance.

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.