Michael Rossmann

Michael G. Rossmann (30 July 1930 – 14 May 2019) was a German-American physicist, microbiologist, and Hanley Distinguished Professor of Biological Sciences at Purdue University who led a team of researchers to be the first to map the structure of a human common cold virus to an atomic level. He also discovered the Rossmann fold protein motif. His most well recognised contribution to structural biology is the development of a phasing technique named molecular replacement, which has led to about three quarters of depositions in the Protein Data Bank.

Education Born in Frankfurt, Germany, Rossmann studied physics and mathematics at the University of London, where he received BSc and MSc degrees. He moved to Glasgow in 1953 where he taught physics in the technical college and received his Ph.D. in chemical crystallography in 1956. He attributes his initial interest in crystallography to Kathleen Lonsdale, whom he heard speak as a schoolboy.

Rossmann began his career as a crystallographer when he became a student of J. Monteath Robertson at the University of Glasgow. The title of his thesis was "A Study of Some Organic Crystal Structures".

In 1956 he and his family moved to the University of Minnesota, where he worked for two years as a post-doctoral fellow with Professor William N. Lipscomb Jr., publishing on the structure of an Iresin Diester

In 1970 his laboratory found the structure of dogfish lactate dehydrogenase, one of the largest early proteins to be solved. In 1973 his group found the structure of Glyceraldehyde 3-phosphate dehydrogenase, and Rossmann immediately realized that the binding site for the NAD+ was very similar to the one in the lactate dehydrogenase. This is now called the Rossmann fold. It is found in enzymes (such as dehydrogenases or kinases) that bind molecules such as ATP or NAD+/NADH.

Rossmann then turned to viruses, spending a sabbatical in 1971 with Bror Strandberg in Uppsala, Sweden, working on the structure of the satellite tobacco necrosis virus. From 1972 to 1980 Rossmann and his team worked on the southern bean mosaic virus. This required developing new software and adapting existing software for Fourier transforms. It was found that this virus had a similar "jelly roll fold" to that found previously in the tomato bushy stunt virus, which at the time was a surprise. The breakthrough nature of this result was such that the National Science Foundation, which provided partial funding for the research, saw fit to organize a press conference, and the news travelled in the general press. This work laid the foundation for a molecular understanding of cell entry of enteroviruses and for the development of capsid-binding inhibitors against a broad range of enteroviruses.

After the success with the first cold virus, work was done on alphaviruses and flaviviruses. This work was made possible by more than one decade of studies on related mosquito borne flaviviruses, including dengue virus, using a combination of cryo-electron microscopy and X-ray crystallography.

Rossmann also had a long-term interest in complicated viral machines. These are exemplified by bacteriophage T4 and nucleocytoplasmic large DNA viruses, also referred to as giant viruses. The determination of an atomic structure of Paramecium bursaria chlorella virus 1 that infects algae has opened up new possibilities for studying giant viruses at the atomic level.

Life and hobbies Rossmann was an avid hiker and sailboat enthusiast, winning M-16 Scow races on Indiana lakes. He was very energetic, which sometimes caused difficulties for his team members. the University of Strasbourg, France; Vrije Universiteit Brussel, Belgium; University of Glasgow, Scotland; University of York, England; Institut Armand-Frappier, University of Québec, Canada. He was awarded the Gregori Aminoff Prize in 1994, the Ewald Prize in 1996, and the Paul Ehrlich and Ludwig Darmstaedter Prize in 2001.

His own employer awarded him with the Purdue University Medal of Honor in 1995.

In 2016, he was awarded the Raymond and Beverly Sackler International Prize in Biophysics for pioneering contributions to high-resolution diffraction analysis of atomic structures of proteins and viruses.