The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding

The crystal structure of the bacteriophage SF6 small terminase DNA-binding domain has been solved at 1.58 Å resolution. A model for the interaction of G1P with the DNA is proposed.

Cloning, expression, purification, crystallization and preliminary X-ray analysis of EaLsc, a levansucrase from Erwinia amylovora

EaLsc, a levansucrase from E. amylovora, has been cloned, expressed, purified and crystallized. X-ray crystallographic analysis and data collection to 2.77 Å resolution have been carried out. The structure was solved by molecular replacement and refinement is in progress.