Michael G. Rossmann (30 July 1930[1] – 14 May 2019)[2] 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.
His most well recognised contribution to structural biology is the development of a phasing technique named molecular replacement,[3] which has led to about three quarters of depositions in the Protein Data Bank.
Born in Frankfurt, Germany, Rossmann studied physics and mathematics at the University of London, where he received BSc and MSc degrees.
[9] 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.
Part of the problem was that it was very difficult at the time to produce milligram quantities of an animal virus, as needed for the X-ray crystallography.
[19] This work was made possible by more than one decade of studies on related mosquito borne flaviviruses, including dengue virus,[20][21][22][23][24] using a combination of cryo-electron microscopy and X-ray crystallography.
When diagnosed with cancer, Rossmann moved into a retirement home, where he met and later married a staff member in charge of welcoming and hospitality, Karen Bogan.
Purdue president (and former Indiana governor) Mitch Daniels said of him, "Still vital, still curious, still in his lab at age 88, his was a life as rich in personal example as it was in scientific achievement.
Calculating electron density structure from X-ray crystallography results by Rossmann's team had long been one of the larger tasks carried out on Purdue's computing systems.
[citation needed] 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.