Michael G. Rossmann

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About

Michael G. Rossmann was a towering figure in structural biology, renowned for his pioneering work in macromolecular crystallography and virus structure determination. His major contributions include the discovery of the Rossmann fold, a ubiquitous protein structural motif critical for nucleotide binding, and the development of molecular replacement methods that revolutionized the field. He led the first X-ray structure determination of a virus (tomato bushy stunt virus) and later solved the structures of numerous human pathogens, including rhinovirus and dengue virus, providing foundational insights for antiviral drug design. His landmark paper "The use of antibody fragments for crystallization and structure determinations" (1995, 70 citations) introduced techniques that enabled the crystallization of challenging proteins. He also co-edited the authoritative *International Tables for Crystallography Volume F* (2001), an essential resource for structural biologists. With over 70,000 citations across his career, Rossmann’s work has had a profound and lasting impact, earning him numerous honors including election to the Royal Society and the National Academy of Sciences. His legacy continues to inspire generations of researchers in structural biology and virology.