Michael was born on 30 July 1930 in Frankfurt, Germany. In 1939, as World War II ignited, he immigrated to England with his mother. He obtained BS and MS degrees from the University of London in mathematics and physics, and he completed his PhD studies in chemical crystallography at the University of Glasgow with J. Monteath Robertson. Michael attributed his interest in crystallography to a pioneer in X-ray diffraction, Kathleen Lonsdale, from whom he first heard about crystallography as a schoolboy. After obtaining his PhD degree, Michael worked with William Lipscomb at the University of Minnesota, where for 2 years he determined structures of terpenoids and wrote computer programs for solving and analyzing structures. After hearing about the exciting project on the structure determination of hemoglobin by Max Perutz from a lecture by Dorothy Hodgkin at the Fourth Congress and General Assembly of the International Union of Crystallography in Montreal in 1957, Michael wrote to and joined Perutz in 1958 at the then Medical Research Council Unit for Molecular Biology, Cavendish Laboratory, University of Cambridge. There, Michael led the computational effort for the structure determination of hemoglobin1, a result that, together with the structure of myoglobin, was recognized with the Nobel Prize in chemistry to Perutz and to John Kendrew, respectively, in 1962.
The time that Michael spent at the Medical Research Council in Cambridge was a seminal period in shaping his scientific vision and career. While working on hemoglobin, Michael noticed the structural similarity between myoglobin and the α- and β-chains of hemoglobin, and he was fascinated by the evolutionary and methodological implications of this observation. He asked himself whether the discovery of a common fold could have been made by a direct comparison of the diffraction patterns of their crystals. In a landmark paper in 1962 with David Blow, Michael demonstrated that the relationship between identical or similar subunits within a crystallographic asymmetric unit can be identified by rotating the Patterson function until it attains a maximal coincidence with the original Patterson, an algorithm called the ‘rotation function’2. Michael and colleagues further established a translation function, also based on the Patterson synthesis, to determine the relative position between the subunits once the rotation is known. The same idea is applicable to finding relationships between identical or similar subunits in different crystals; this molecular replacement method that uses a known structure to solve similar but unknown structures in new crystals later became the most frequently used tool for solving macromolecular crystal structures and currently accounts for about 85% of all new structures deposited in the Protein Data Bank.
