The first structure of a glycerol kinase from the parasite T. cruzi with a bound glycerol molecule is presented.

The crystal structure of the MIF4G domain of Trypanosoma cruzi EIF4G5 reveals differences that may account for the specific interaction mechanisms of MIF4G.

The structures of T. brucei brucei adenosine kinase in open and closed conformations give insight into the substrate-binding mode and can be used to improve the properties of antitrypanosomal agents.

The production, purification and crystallization of a recently identified trans-sialidase from T. vivax is described. The purified enzyme is active and produces diffraction-quality crystals using the sitting-drop vapour-diffusion method. The crystals belonged to space group P2₁2₁2₁ and diffracted to 2.5 Å resolution.

In this study, a structural approach was used to unveil the molecular function of ZC3H41, an essential yet enigmatic protein in the life cycle of T. brucei. Here, the expression, purification and crystallization of this protein are reported.

X-ray structural analysis of T. cruzi spermidine synthase was conducted to identify novel inhibitor-binding sites, including an allosteric site, and to elucidate inhibition mechanisms.

Structural insights into the development of a tricyclic compound as an inhibitor of Trypanosoma brucei pteridine reductase 1 are reported.

Structures of aspartate aminotransferases from eukaryotic pathogens were solved in complex with pyridoxal phosphate. The four structures show either the open or the closed conformation of the enzyme.

A quinary multi-hexameric helical structure of T. cruzi NDPK1 is supported by crystallographic and in vivo studies.

Superoxide dismutases (SODs) catalyze the conversion of superoxide to molecular oxygen, thus protecting organisms against toxic radicals. Iron-dependent SODs from T. cruzi, L. major and B. bovis exist as multiple isoforms with distinct structural features.