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About

Raymond C. Stevens is a pioneering structural biologist whose work has fundamentally advanced the field of protein crystallography and structural genomics. His research sits at the intersection of automation, methodology development, and structural biology, with a particular focus on making high-resolution protein structure determination faster, more reliable, and more accessible to the broader scientific community. Stevens is perhaps best recognized for his contributions to automating the crystallography pipeline. His 2004 paper on automated sample mounting and alignment systems for biological crystallography at synchrotron sources garnered over 100 citations, reflecting how transformatively this work accelerated structural biology workflows worldwide. Complementing this, his 2003 work on robotics for automated crystal formation and analysis helped lay the groundwork for high-throughput structural genomics. His structural studies of enzymes from the thermophilic bacterium *Thermotoga maritima* — including γ-glutamyl phosphate reductase and uronate isomerase — provided atomic-level insights into metabolic enzymes involved in proline biosynthesis and sugar isomerization, contributing to our understanding of thermostable protein architecture. His forward-looking 2007 contribution on generating protein structures for the 21st century further underscores his commitment to shaping the future of structural biology infrastructure and methodology.