The crystal structure of an epoxide hydrolase from Streptomyces sp. CBMAI 2042 was determined and revealed the conserved overall fold found in other α/β-hydrolases, despite its unusual hexameric quaternary structure. Although its primary sequence is similar to that of a Mycobacterium tuberculosis epoxide hydrolase, its active-site architecture, and particularly its volume, closely resembles the human epoxide hydrolase.

In this work, serial crystallography is applied to a drug discovery target and the room-temperature ligand-bound complexes are used to explore temperature-dependent structural differences.

The P. aeruginosa virulence factor Cif, which inhibits cell-surface expression of the cystic fibrosis transmembrane conductance regulator, has been expressed, purified and crystallized.

By switching from hanging-drop experiments to liquid-liquid diffusion in capillaries, well diffracting crystals could be obtained for leukotriene A₄ hydrolase from S. cerevisiae.

L-Azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C was crystallized and diffraction data were collected to a resolution of 1.38 Å.

The crystal structure of Rv0554 from M. tuberculosis has been determined, revealing a dimeric protein with an α/β-hydrolase fold. Functional assays failed to support a proposed role in menaquinone biosynthesis.

Progress in the determination of structures of human proteins by the Structural Proteomics In Europe (SPINE) consortium is outlined with highlights indicating the impact of high-throughput technologies.