Aina E. Cohen

The paper develops a graphene device for high-temperature crystallography to study enzymatic reactivity across temperature ranges, revealing how transition state ensembles relate to catalytic rates.

The paper introduces CAGE-TRX, a method for time-resolved crystallography that uses photocaged amino acids to control enzyme activity and capture reaction intermediates.

This study uses time-resolved crystallography to capture GTP hydrolysis intermediates of N-RAS and oncogenic mutants, revealing shared and distinct reaction mechanisms.

This study shows that shipping protein crystals at room temperature across long distances does not compromise diffraction quality for in situ X-ray diffraction experiments.

The paper determines the structure of active Ni(I)-Methyl-CoM reductase, revealing how it catalyzes methane formation and providing insights for methane emission control and biofuel production.

This paper describes a scalable microfluidic device for automated X-ray crystallography that enables efficient and damage-free crystal mounting for protein structure analysis.

This paper presents the structure of ATP-bound RNA Polymerase II at 3.0 Å resolution using a free-electron laser, revealing new insights into substrate binding and metal coordination in the active site.

The paper uses XFEL crystallography to observe conformational changes in an enzyme during catalysis, revealing ionization-linked dynamics that control catalytic activity.

This paper determines the structure of Escherichia coli dGTPase and elucidates the molecular basis of its dGTP selectivity through comparative analysis with SAMHD1.