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 and a terpenoid, and writing computer programs for analysing structures. Career 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 directed the Purdue X-ray crystallography laboratory. He became full professor in 1967 and from 1978 held the chair of Hanley Distinguished Professor of Biological Sciences at the university. He also held 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 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