Ehmke Pohl

European Molecular Biology Laboratory, Durham University

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About

Ehmke Pohl is a leading structural biologist whose work bridges synchrotron instrumentation and macromolecular crystallography. His research centers on developing automated beamline technologies and solving the three-dimensional structures of regulatory proteins critical to bacterial pathogenesis. A major contribution is his pioneering role in automating the EMBL Hamburg protein crystallography beamline BW7B at the DORIS III synchrotron, a fixed-energy beamline that receives half the radiation from a 56-pole wiggler. This work, cited 49 times, significantly advanced high-throughput data collection for the structural biology community. Pohl also made key discoveries in bacterial gene regulation, most notably determining the crystal structure of the caseinolytic protease gene regulator ClgR from *Corynebacterium glutamicum* (18 citations). This transcriptional activator controls the expression of ClpCP protease genes, which are essential for virulence in human pathogens like *Mycobacterium tuberculosis* and *Corynebacterium* species. By revealing how ClgR binds pseudo-palindromic operator DNA, Pohl provided molecular insights into antibiotic target pathways. His dual expertise—optimizing synchrotron infrastructure and decoding pathogen regulatory mechanisms—makes his work foundational for both structural biology methods and infectious disease research.