Biographical/historical note written with reference to Oxford DNB.

Johnson, Dame Louise Napier (1940–2012), biophysicist and structural biologist, was born 26 September 1940 in Worcester. Educated at Wimbledon High School for Girls, she went on to University College, London in 1959, obtaining a BSc (Hons) in Physics in 1962.

She carried out her doctoral research on substrate binding at the Royal Institution, London under the supervision of David Phillips, whose team was working on the structure of the enzyme lysozyme using x-ray scattering techniques. Completing her PhD thesis in 1965, her work was published in Nature and led to the first understanding--at the structural level--of the mechanism of action of an enzyme. She spent a short time at Yale University as a post-doctoral researcher under Fred Richards before returning in 1967 to join David Phillips’ newly formed Laboratory of Molecular Biophysics at Oxford University.

In Oxford, Johnson became a departmental administrator in the Zoology Department and Janet Vaughan Lecturer in Biophysics at Somerville College. In 1973 she became a university lecturer and additional fellow of Somerville College.

Realising the potential of synchrotron radiation, Johnson’s group was at the forefront of its use in the 1980s for macromolecular crystallography. Her pioneering work on glycogen phosphorylase and cell cycle regulatory proteins transformed understanding of not just large protein structures but how they worked as complex biochemical machines.

Upon Phillips’ retirement in 1990 Johnson was made the David Phillips Professor of Molecular Biophysics and took over as head of the Laboratory of Molecular Biophysics. She also became a professorial fellow of Corpus Christi College while remaining an honorary fellow of Somerville. She held these posts until her retirement in 2007.

She was elected a fellow of the Royal Society in 1990 and a member of the European Molecular Biology Organization the following year.

In 2003 she became the Life Sciences Director at Diamond Light Source; helping to lead the development of the UK’s national synchrotron and promoting its application to questions in structural biology. Her tireless work saw the establishment of the Membrane Protein Laboratory at Diamond and the Research Complex at Harwell for visiting researchers. She was made a Diamond fellow after her retirement in 2008.

On an international level Johnson supported the establishment of research laboratories in developing regions, made numerous trips to give lectures and advise scientists in developing countries and promoted projects such as the Synchrotron Light for Experimental Science and Applications in the Middle East (SESAME), which offered a unique opportunity for scientists across the Middle East to work together.

During her long career, Johnson authored or co-authored 186 peer-reviewed scientific papers as well as served on many advisory committees the world over. Her book with Tom Blundell, Protein Crystallography (1976) is considered a classic in the field and she was the recipient of numerous honours and honorary degrees. Johnson was incredibly supportive of young scientists, particularly women, and understood the challenges of juggling a scientific career with family life. She encouraged a family-friendly work ethic and cooperative working environment that trained a generation of crystallographers in Oxford. She herself married in 1968 the theoretical physicist and future Nobel laureate Muhammad Abdus Salam (1926-1996) and had a son Umar (b. 1974) and a daughter Sayyeda (b.1982). After her retirement she moved to Cambridge in 2011 to be with her son and his family. She died at Addenbrooke’s Hospital in Cambridge on 25 September 2012 and was cremated on 6 October of that year at Cambridge city crematorium.