Michael Rossmann

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.

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Education

Born in Frankfurt, Germany, Michael 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.^[1].

Michael 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 with Professor William Lipscomb, publishing several papers on the structure of terpenoids and writing computer programs for analysing structures. He returned to England and to the University of Cambridge in 1958, where he worked with Max Perutz on the structure of haemoglobin. He went to Purdue in 1964.

Career

He worked as a post-doctoral fellow at the University of Minnesota with Professor William Lipscomb and as research associate at the MRC Laboratory of Molecular Biology in Cambridge, England , where he worked with Max Perutz on the structure of haemoglobin. In 1964, he joined the faculty of the Department of Biological Sciences at Purdue as an associate professor and has been there since.

Michael Rossmann directs the X-ray crystallography laboratory at Purdue University. 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 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.^[2]

In 1973 Rossman published the decription of the Rossman fold, a nucleotide binding motif found in enzymes such as dehydrogenases or kinases that bind molecules such as adenosine triphosphate or nicotinamide adenine dinucleotide.^[3]

In 1985, he published his team's mapping, using X-ray crystallography, of a human common cold virus in the journal Nature^[4]. 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.^[5]

Awards and Honors

Among other honors, Michael Rossmann has been elected Fellow of the American Academy of Arts and Sciences in 1978, Member of the National Academy of Sciences in 1984, Foreign Member of the Royal Society of London in 1996, and Fellow of the American Association for the Advancement of Science in 1999.

He was awarded honorary doctorates by the University of Uppsala, Sweden; the University of Strasbourg, France; Vrije Universiteit Brussel, Belgium; University of Glasgow, Scotland; University of York, England; Institut Armand-Frappier, University of Québec, Canada.

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

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