The structure of the haloalkane dehalogenase DpcA from the psychrophilic bacterium Psychrobacter cryohalolentis K5, an attractive enzyme for biotechnological applications, was solved at the atomic resolution of 1.05 Å. The enzyme possesses main and slot tunnels with the shortest lengths in comparison with other haloalkane dehalogenases. Structural comparisons show major differences in the region of the α4 helix of the cap domain, which is one of the determinants of the properties of the tunnels. The structural information on DpcA establishes a basis for understanding its catalytic properties and can guide the modification of this cold-adapted enzyme for various biotechnological applications.

Biochemical and structural features of the cold-adapted Acinetobacter sp. Ver3 catalase KatE1 are reported.

The adaptation of enzymes to low temperatures and seawater salinity has been investigated on a structural level. The crystal structure of V. salmonicida endonuclease I is presented and compared with the corresponding enzyme structures from V. cholerae and V. vulnificus.

The first crystal structures of a dimeric, cold-adapted β-D-galactosidase from Paracoccus sp. 32d and its complex with galactose were determined. The atypical arrangement of domains may be one of the factors that are responsible for the creation of a functional dimer of this enzyme.

Crystals of the aspartate carbamoyltransferase of the psychrophile M. profunda diffract X-rays to 2.85 Å. Three catalytic and three regulatory subunits are predicted per asymmetric unit.

The 1.7 Å crystal structure of the non-psychrophidic cationic salmon trypsin comprise 4 molecules per asymmetric unit. The four independently refined molecules are compared to each other to the cold-adapted anionic salmon trypsin and the bovine trypsin, to search for the structural basis of the psychrophilic trypsin

Monoclinic (P2₁) crystals of a His-tagged form of V. salmonicida catalase without cofactor diffract X-rays to 1.96 Å.

The catalytic core domain of the psychrophilic cellulase CelG from P. haloplanktis has been crystallized and diffraction data have been collected to 1.8 Å.

X-ray crystal structures were determined of the wild type and an inactive mutant of α-amylase from the earthworm Eisenia fetida. Structural analyses reveal the molecular properties that are responsible for catalytic activity at low temperatures and substrate recognition.

The crystallization and preliminary X-ray analysis of a cold-active endo-β-1,4-D-xylanase is described. The crystals diffracted to 2.7 Å resolution.