Michael Beer

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 study uses molecular dynamics simulations to identify structural features distinguishing carbapenemase activity in class A β-lactamases.

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.

This paper introduces a D-NEMD method to identify allosteric positions in proteins by analyzing long-range structural responses to alanine substitutions, validated on KPC-2 beta-lactamase.

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 investigates how electric fields in class A β-lactamases influence carbapenemase activity using molecular dynamics simulations and identifies key positions that correlate with enzyme efficiency.

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