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About

Christian Cambillau is a structural biologist whose research spans bacteriophage biology, structural genomics, and chemical ecology, with particular expertise in protein crystallography and structural determination. His most celebrated contribution lies in elucidating the molecular architecture of bacteriophages that threaten dairy fermentation, most notably his 2006 study revealing the modular structure of receptor-binding proteins in *Lactococcus lactis* phages — work that has garnered over 113 citations and carries significant implications for protecting industrial dairy production from phage contamination. Cambillau has also made meaningful contributions to the field of structural genomics, championing a medium-throughput crystallization methodology that streamlined the transition from protein to crystal structure through a two-step robotic screening and optimization pipeline, accumulating 80 citations and influencing laboratory workflows worldwide. His structural interests extend into insect chemical ecology, where he pursued the crystallographic characterization of pheromone-binding proteins from species including the honeybee *Apis mellifera* and the cockroach *Leucophaea maderae*, illuminating the molecular basis of olfactory signaling. His structural genomics efforts additionally uncovered unexpected homologies in bacterial proteins of unknown function, exemplified by his work on *E. coli* yddE. Across these diverse systems, Cambillau's career reflects a sustained commitment to using crystallography as a discovery tool.