This study presents the crystal structure of the trifunctional THI20 from S. cerevisiae, an enzyme with an N-terminal HMP kinase (ThiD-like) domain and a C-terminal thiaminase II (TenA-like) domain. In addition, two distinct structural classes of TenA have been identified by comparison to other known structures.

Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme have resulted in 121 binding events of 16 out of 226 investigated fragments, suggesting functional sites with respect to substrate binding and substrate channeling.

The catabolism of fatty acids in mycobacteria involves an extensively redundant set of enzymes. Here, the structure of the L-3-hydroxyacyl-CoA dehydrogenase FadB2 is described and structural cues as to how it may work with other components of β-oxidation are explored.

The X-ray structure of human bisphosphoglycerate mutase was solved to 1.94 Å resolution and a bisphosphoglycerate mutase-citrate model was built to explore enzyme-inhibitor interactions.

The first diffraction-quality crystals of a PutA protein are reported. One of the three crystal forms described here exhibits pseudo-merohedral twinning. Removal of the N-terminal histidine tag aided the crystallization of another form.

The dihydroorotase domain from hamster was crystallized by vapour diffusion. The crystals were found to exclusively consist of a disulfide-linked tetrameric form of the enzyme.