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D.K. Stammers is a structural biologist whose research has significantly advanced our understanding of protein crystallization and enzyme mechanisms, particularly in the context of drug discovery. His work is defined by two major contributions: pioneering high-throughput crystallization methods and elucidating the structure of key biosynthetic enzymes. Stammers co-developed a robotic system for nanolitre-scale crystallization, dramatically reducing the sample volume required for protein structure determination. A landmark 2003 paper, cited over 130 times, presented the first systematic results from this approach, demonstrating its reliability across more than 50 diverse protein samples and establishing a new standard for efficiency in structural genomics. This work has had a lasting impact on how laboratories worldwide approach protein crystallography. Complementing this methodological innovation, Stammers solved the structure of GTP cyclohydrolase II, an enzyme essential for riboflavin biosynthesis. His 2005 study revealed the enzyme’s unique mechanism and highlighted its potential as a target for novel antimicrobials, given its absence in humans. By combining technical ingenuity with fundamental biological insight, Stammers has made enduring contributions to both the practice and application of structural biology.