The crystal structure of the hydratase from Lactobacillus acidophilus (LAH) has been determined by single-wavelength anomalous dispersion. Crystal structures of apo LAH and of LAH with bound linoleic acid were refined at resolutions of 2.3 and 1.8 Å, respectively.

(R)-Hydratase from A. caviae involved in PHA biosynthesis has been crystallized in space group C2, with unit-cell parameters a = 111.54, b = 59.29, c = 47.27 Å, β = 113.04°.

The gene encoding HpcG from the homoprotocatechuate (4-hydroxyphenylacetic acid) degradative pathway of E. coli C has been cloned and expressed and the protein has been purified. Crystals obtained from the purified recombinant enzyme, belonging to a tetragonal space group, diffracted to a resolution of 2.1 Å.

Fumarate hydratase is an enzyme of the tricarboxylic acid cycle, one of the metabolic pathways characteristic of the mitochondria. The structure of R. prowazekii class II fumarate hydratase is reported at 2.4 Å resolution and is compared with the available structure of the human homolog.

The MaoC-like dehydratase from P. capsici was cloned, expressed and purified to homogeneity. Crystals were obtained that diffracted to 1.93 Å resolution.

Recombinant human fumarase has been overexpressed in E. coli and crystallized in the presence of polyethylene glycol as a precipitant agent. The structure was solved by molecular-replacement techniques.

A CN-hydrolase superfamily protein from the plant pathogen X. campestris has been overexpressed in E. coli, purified and crystallized.

The analyses of the crystal structure of Nm23-H1 combined with H/D exchange experiments under oxidative condition revealed an intramolecular disulfide bond triggering a large conformational change that destabilizes the hexameric state and provides an environment for the oxidation of Cys109 to sulfonic acid.

The structure of S. aureus MenB, an enzyme in the biosynthetic pathway to vitamin K₂, has been determined and compared with the enzyme derived from another important pathogen, M. tuberculosis.