The first user experiment on FabG-NADP complex at BioMAX was carried out by Peter Vella, Robert Schnell, Gunter Schneider at the Division of Molecular Structural Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
The crystal structure of FabG from Acinetobacter baumannii was determined to 1.8 Å resolution from x-ray diffraction data collected at the MAX IV BioMAX beamline. FabG is part of the bacterial fatty acid biosynthesis machinery and is considered as one of the few essential proteins from Gram-negative bacteria that are validated targets for antibiotic development.
The spread of antibiotic resistance in human pathogens complicates the treatment of infections and new antibacterial drugs with novel mechanisms are needed to counteract the present drug resistant infections. Detailed biochemical information and the high resolution structures of the target proteins facilitate the development of inhibitors and antibiotics with established mechanism of action.
The tetramer of FabG with the cofactor NADP bound in each active site (left), and the 2Fo-Fc electron density map of the NADP ligand contoured at 1σ (right)
Interview with Thomas Ursby, Researcher at BioMAX, about the first users at the beamline, the research that will be made at BioMAX and the future of MAX IV.