Expression, purification, crystallization and preliminary crystallographic analysis of a thermostable DNA ligase from the archaeon Thermococcus sibiricus

A recombinant ATP-dependent DNA ligase from the hyperthermophilic anaerobic archaeon Thermococcus sibiricus was expressed in Escherichia coli and purified. Crystals were grown by vapour diffusion using the hanging-drop method.

Influence of intermolecular contacts on the structure of recombinant prolidase from Thermococcus sibiricus

The structure of recombinant prolidase from the hyperthermophilic archaeon Thermococcus sibiricus (Tsprol) was determined at 2.6 Å resolution.

Crystallization of uridine phosphorylase from Shewanella oneidensis MR-1 in the laboratory and under microgravity and preliminary X-ray diffraction analysis

High-quality crystals of uridine phosphorylase from Shewanella oneidensis were grown under microgravity conditions. X-ray diffraction data were collected to a resolution of 0.95 Å.

ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain

The structure of ATP-dependent DNA ligase from Thermococcus sp. 1519 was determined at a resolution of 3.02 Å, showing a new relative arrangement of the OB-fold domain.