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About

Ashley M. Deacon is a structural biologist whose research sits at the intersection of crystallography automation, synchrotron technology, and structural genomics. Working primarily at the Stanford Synchrotron Radiation Laboratory (SSRL) and the Joint Center for Structural Genomics (JCSG), Deacon has made pivotal contributions to modernizing how protein crystal structures are determined at scale. Deacon's most celebrated achievement — garnering 262 citations — was the development of an automated robotic system for mounting cryo-cooled protein crystals on synchrotron beamlines. By combining a compact industrial robot with standardized 96-crystal cassettes, this innovation dramatically accelerated high-throughput crystallography and became foundational infrastructure for structural biology facilities worldwide. Complementing this, Deacon contributed to infrared imaging techniques for locating crystals in cryoloops, an elegant solution to a persistent practical challenge in sample handling. Within the structural genomics arena, Deacon contributed to the JCSG's automated structure-solution pipeline, Xsolve, enabling distributed, large-scale protein structure determination. His crystallographic work also yielded solved structures of enzymes from the extremophile *Thermotoga maritima*, including γ-glutamyl phosphate reductase and uronate isomerase, advancing understanding of metabolic pathways in thermophilic organisms. Collectively, Deacon's work has helped transform structural biology into a more automated, efficient, and accessible discipline.