Max Perutz (1914–2002)

Become a scientist, Ernest Rutherford would urge his friends, for then you will never be old, you will remain all your life a child at play. So it proved for the evergreen Max Perutz, who did his last experiment only weeks before he died at the fine age of eighty-seven. Perutz embraced Noël Coward's dictum that 'work is fun, work is much more fun than fun'. In an eventful life, beset in its early years with fluctuating fortune, adversity and sometimes danger, the transcendent moments of true drama, of which he wrote with such charm and immediacy, came in the laboratory. One Saturday morning in 1951, browsing in the library, Max opens the latest issue of the Proceedings of the National Academy of Sciences and there finds the famous paper by Pauling and Corey in which the α α-helix stands revealed. Appalled at his failure to discern such a fundamental structural principle in his own X-ray and model-building studies, he pedals home in a daze. Deaf to the clamour of his young family, he broods as he swallows his lunch. And of a sudden, inspiration strikes: the configuration of the diffraction experiments was such that they could not have revealed the 1.5 Å reflection that the structure demanded. Back to the lab, then; Perutz fishes for a horse hair in his desk drawer, sets up the experiment and develops the film in a lather of impatience, and there is the reflection — Pauling's helix made manifest in the developer dish. Another such moment came after twenty years of inconclusive toil on the crystal structure of haemoglobin, the molecule to which Perutz consecrated his life. The principle of isomorphous replacement came in a flash of insight. He immediately prepared a mercury derivative of his protein and, lo! the diffraction picture showed exactly what he had hoped: the spots were in the same place, but the relative intensities were altered. He must have realised in that moment that he would eventually run his elusive quarry to earth. And best of all, in 1961, the long-sought structure at last came into view, with its helices, its haem groups with their ligands, everything, in short, about which protein chemists had argued and speculated for decades. For those who were privileged to be around when the oxyhaemoglobin structure was unveiled (along with Kendrew's myoglobin) it came as an epiphany: we were witnesses to a historic …