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About

Jessica L. Thomaston is a structural biologist whose work has significantly advanced the study of membrane proteins, particularly those involved in viral infection and drug resistance. Her research centers on developing innovative crystallographic techniques to overcome the challenges of working with small, radiation-sensitive crystals, enabling high-resolution structural determination of dynamic biological targets. She is best known for her contributions to the design of "high-density grids" for efficient data collection from multiple crystals (75 citations), a method that has become essential for productive femtosecond crystallography at X-ray free-electron lasers and microfocus synchrotron beamlines. Through this work, Thomaston has enabled the structural characterization of influenza A M2 proton channel inhibitors and other pharmaceutically relevant membrane proteins, providing critical insights into drug binding and resistance mechanisms. Her methodological innovations have directly impacted the broader structural biology community, facilitating studies of previously intractable targets. With a citation count reflecting the utility of her approaches, Thomaston stands out for her ability to bridge cutting-edge technology and fundamental biological questions, making her a key figure in the push toward more efficient, high-throughput structural biology.