Scientific projects of the IBS synchrotron group

We investigate the structure and dynamics of diverse macromolecules, with a strong focus on fluorescent proteins and metabolic enzymes. Our work on fluorescent proteins spans classical GFP homologs (Cerulean, mScarlet), bacterial phytochrome-derived near-infrared proteins (mIFP), and variants such as mEmerald, where combined spectroscopy and crystallography are used to probe phototransformations under controlled radiation conditions. In parallel, we explore enzymes from the MEP pathway, a key target for antibacterial drug discovery, through fragment-based ligand screening and structure determination. We also study large aminopeptidases (TET) using room-temperature and variable-temperature crystallography to capture conformational dynamics. Beyond biological targets, we develop methodologies and instrumentation, including room-temperature and high-pressure crystallography, and high-throughput ligand screening, to expand structural biology applications in biotechnology.