Structure of Plasmodium vivax N-myristoyltransferase with inhibitor IMP-1088: exploring an NMT inhibitor for antimalarial therapy

The 1.8 Å resolution ternary structure of P. vivax N-myristoyltransferase in complex with IMP-1088 and myristoyl-CoA is presented. IMP-1088 is an N-myristoyltransferase inhibitor from a family of inhibitors that are under investigation as antimalarials.

Co-crystal structure of Helicobacter pylori biotin protein ligase with biotinyl-5-ATP

Recombinant N-terminally histidine-tagged H. pylori biotin protein ligase was purified and its 2.25 Å resolution co-crystal structure with biotinyl-5-ATP is reported.

Small-angle X-ray scattering of engineered antigen-binding fragments: the case of glycosylated Fab from the Mannitou IgM antibody

This study provides a biochemical and biophysical analysis of Mannitou Fab, highlighting the intricate balance between stability, flexibility and function in engineered antibody fragments. The results underscore the critical role of glycosylation in modulating the oligomerization behaviour of Fab and preventing inappropriate intermolecular interactions, paving the way for more effective and reliable therapeutic antibodies in the future.

Crystallization and preliminary X-ray crystallographic studies of AfeH from Acimetobacter sp. DL-2

X-ray diffraction data for AfeH were collected to 1.9 Å resolution. Further structural determination will pave the way for the rational design of AfeH.