Mouse ketohexokinase A undergoes a conformational change during the catalytic cycle. The conformational change is consistent between the two isozymes, A and C, and across species.

A device and method for gentle, automated and inexpensive solution exchange for macromolecular crystals is described.

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The crystal structure of HNL6V, a seven-substitution variant of hydroxynitrile lyase from rubber tree, reveals that engineered mutations designed to mimic the homologous esterase SABP2 shift the catalytic atom positions intermediate between those of the parent enzyme and the target esterase.

We determined high-resolution crystal structures of the histone deacetylase inhibitor vorinostat bound to both human carbonic anhydrase II and a carbonic anhydrase IX active-site mimic. Thermal shift assays using differential scanning fluorimetry showed minimal stabilization of either carbonic anhydrase by vorinostat, in contrast to the potent carbonic anhydrase inhibitor acetazolamide.

The high-resolution crystal structure of triosephosphate isomerase from F. hepatica was solved at 1.51 Å resolution in its monoclinic form, revealing details of the dimer interface critical for enzyme function. Molecular docking with the fasciolocide triclabendazole suggests selective binding near nonconserved residues, highlighting this enzyme as a promising parasite-specific drug target.