Dame Louise Napier Johnson (1940–2012)

One of the pioneering spirits of protein crystallography has passed away. Professor Louise Napier Johnson, DBE, FRS, died on 25 September 2012, the day before her 72nd birthday. Throughout her career Louise was a leading figure, applying an incisive physics intelligence to problems in biology. Many years later she assumed leadership roles at Oxford University and at the Diamond synchrotron in Oxfordshire, but never lost her delight in science and unassuming kindness towards those around her, to whom she was a remarkable example. As early as 1934, J. D. Bernal and Dorothy Hodgkin had shown that it might be possible to decipher the structures of proteins using X-ray crystallography, and, working in Cambridge, initially overseen by Sir Lawrence Bragg, John Kendrew and Max Perutz eventually determined the first protein structure in the late 1950s. Enzymes remained uncharted, but in 1962 not only were Kendrew and Perutz awarded the Nobel Prize but, armed with a degree in physics from University College London, Louise started a PhD at the Royal Institution where Lawrence Bragg had moved from Cambridge. She joined a new group led by David Phillips, later Lord Phillips of Ellesmere [Perutz (1999). J. Synchrotron Rad. 6, 945–946], which had set itself the task of explaining the mystery of enzymes using X-rays. They fortuitously chose lysozyme, an enzyme discovered by Alexander Fleming which breaks down the wall around bacterial cells, giving it anti-bacterial properties. Louise took the story to a new level, entering the international stage at a meeting at the Royal Institution in 1965. The three-dimensional structure of the first enzyme was revealed in all its glory, with Louise presenting her analysis of its complexes with N-acetylglucosamine and tri-N-acet-ylglucosamine to show how they beautifully complemented the deep groove across the enzyme's surface and rationalized a wealth of biochemical data [Blake et al. This was the first use of the difference-map technique, apart from for heavy-atom location. Phillips then used model building to extend Louise's results, inferring a detailed mechanism for how the enzyme actually facilitated chemical change, founding structural enzymology. Despite early opposition, this is now accepted as the gold standard framework for understanding enzyme function. Furthermore, the methodology developed for lysozyme became a fundamental pillar of the pharmaceutical industry; indeed, many drugs currently on the market arose in some part through structural analysis of proteins. After the Royal Institution, Louise spent a short postdoctoral spell at Yale, researching ribo-nuclease …