forthcoming articles

High-throughput protein crystallography is used at the heart of a pipeline to accelerate the discovery of bioactive natural products, by capturing these hits with protein crystals directly from unpurified biota samples.

The crystal structure of UmaA from Mycobacterium tuberculosis was solved to 1.95 Å in the space group P3₂21.

The co-crystal structures of five sulfonamide ligands bound to the active site of the IspF enzyme from B. psuedomallei are reported. The ligands include the drugs ethoxzolamide, acetazolamide, sulfapyridine and sulfamonomethoxine.

The crystal structures of tryptophanyl-tRNA synthetase from N. gonorrhoeae were solved in both its apo form and in complex with tryptophan to resolutions of 2.25 and 2.5 Å, respectively. These structures reveal conserved catalytic motifs and conformational changes at the active site upon ligand binding. Additionally, structural comparisons suggest that indolmycin may act as a competitive inhibitor, offering potential for antibiotic development.

The 1.75 Å resolution structure of the G. haemolysans M26 IgA1 protease trypsin-like domain is presented. The structural data suggest that the domain exists in an inactive pro-enzyme-like state when in the context of the full-length protein. This putative pro-enzyme may be activated after being N-terminally excised from the larger M26 enzyme structure through the potential stabilization of its S1 pocket and rearrangement of adjacent surface loops.