Lecture screening in Great Zoological Hall: A Personal History of Structural Virology
Michael G. Rossmann (born 1930) is 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.
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 and a terpenoid, and writing computer programs for analysing structures.
Rossmann returned to the UK and to the University of Cambridge in 1958, where he worked with Max Perutz on the structure of hemoglobin as a research associate at the MRC Laboratory of Molecular Biology.
In 1964 Rossmann joined the faculty of the Department of Biological Sciences at Purdue University as an associate professor. He directs the Purdue X-ray crystallography laboratory. He became full professor in 1967 and since 1978 has held the chair of Hanley Distinguished Professor of Biological Sciences at the university. He also holds a joint appointment in the department of biochemistry and adjunct positions in Cornell University's Division of Biological Sciences and in Indiana University's school of medicine.
In 1973 Rossmann published the description of the Rossmann fold, a nucleotide binding motif found in enzymes such as dehydrogenases or kinases that bind molecules such as adenosine triphosphate or nicotinamide adenine dinucleotide.
In 1985, he published his team's mapping, using X-ray crystallography, of a human common cold virus in the journal Nature. 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.
The Rossmann cluster is named for Michael Rossmann, Purdue's Hanley Distinguished Professor of Biological Sciences, who is a pioneer in employing high-performance computing in research to reveal the structure of viruses and their component protein molecules. Rossmann gained worldwide attention in 1985 by determining the structure of human rhinovirus serotype14, HRV-14, one of about 100 known cold virus strains.