Protein expression, characterization, crystallization and preliminary X-ray crystallographic analysis of a Fic protein from Clostridium difficile

A Fic protein from the pathogenic bacterium C. difficile R20291 has been cloned, expressed and purified. The purified protein was characterized by mass spectrometry and circular-dichroism spectroscopy, and was crystallized. In addition, a diffraction data set was collected and processed to 1.68 Å resolution.

Structures of a human blood group glycosyltransferase in complex with a photo-activatable UDP-Gal derivative reveal two different binding conformations

The structure of AA(Gly)B, a dual-specificity blood group synthase, in complex with UDP-galactose, the O6'' atom of which is protected by an 2-nitrobenzyl group, has been determined in two space groups. The so-called caged substrate exhibits various distinct conformations in the active site.