The structure of the A. fumigatus old yellow enzyme EasA was determined to 1.8 Å resolution. This enzyme catalyzes the reduction of chanoclavine-I aldehyde to dihydrochanoclavine aldehyde and works in conjunction with festuclavine synthase at the branchpoint for ergot alkaloid pathways.

Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the DNA-binding effector domain from an atypical OmpR response regulator homolog, ChxR, encoded by Chlamydia trachomatis are reported.

Retinal dehydrogenase type II was purified from an E. coli overexpression system and crystallized in two separate conditions. Two crystal forms were obtained. Only the crystals belonging to space group P2₁2₁2₁, grown in conditions which minimize O₂ exposure, produced high quality X-ray diffraction data.

Human liver pyruvate kinase converts phosphoenolpyruvate to pyruvate in the final step of glycolysis and is allosterically activated by fructose-1,6-bisphosphate. The allosteric site is located between the phosphate-binding loop and the allosteric loop. The crystal structures of four site-directed mutants revealed a conformational toggle between the open and closed positions of the allosteric loop.

The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 Å resolution.