Spotlight on Louise Johnson

Professor Frank James explores the life of Louise Johnson, the molecular biologist and pioneer of structural enzymology.

  • lysozyme model

    The structure of lysozyme

    Credit: Paul Wilkinson, Ri

In 2014 the Ri is proud to celebrate women in science with the first ever all women line-up for our Friday Evening Discourses. To coincide with these monthly events, Frank James will tell the stories of some of the many women associated with the Ri since 1799 in this monthly blog.

Pratibha Gai will present the next Friday Evening Discourse 'Atoms in action', 8pm to 9.15pm on Friday 27 June. Book your tickets now.

Louise Johnson (1940-2012)

Louise Johnson was born in Worcester on 26 September 1940. From 1952 until 1959 she attended Wimbledon High School for Girls, one of the leading grant maintained schools in the country, where she concentrated on the sciences, although with limited resources for practical work. At University College London she studied physics where she was one of four women out of a class of forty.

After graduating in 1962, she joined the group at the Davy-Faraday Research Laboratory (DFRL) at the Royal Institution to determine the structure of lysozyme. Alexander Fleming discovered lysozyme at St Mary’s Hospital in 1922. He realised lysozyme had anti-microbial properties and spent much time studying it. He later believed that lysozyme was his most important discovery since it provided him with much of the knowledge, skills and techniques that he later brought to his work on penicillin.

The DFRL was directed by Lawrence Bragg who with his father just before the Great War had shown how X-rays could be used to determine the molecular structure of crystals. This was one of the key scientific discoveries of the twentieth century, for which they won the Nobel Prize for Physics in 1915. In the following fifty years the impact of their work had been immense, including the proposal made in 1953 at the Cavendish Laboratory in Cambridge (then directed by Bragg) by Francis Crick and James Watson that the structure of DNA was a double helix. Under Bragg, the lysozyme group was led by David (later Lord) Phillips who had joined the laboratory in 1955. In the late 1950s Phillips and his colleague Uli Arndt invented the linear diffractometer which hugely increased the amount of X-ray crystallographical data that could be gathered automatically. This instrument allowed John Kendrew to work out the structure of myoglobin, for which he won the Nobel Prize for Chemistry in 1962.

  • Louise Johnson photo - wellcome

    Dame Louise Johnson 

    Credit: Anne-Katrin Purkiss, Wellcome Images

  • The structure of lysozyme

    The structure of lysozyme

    Credit: Paul Wilkinson, Ri

Whilst working during a vacation at the Atomic Energy Authority at Harwell, south of Oxford, Johnson met Arndt and learned of the highly active and innovatory research group at the DFRL. In addition to using the linear diffractometer for her work on lysozyme, in 1963 she was given access to an Elliott 803 computer (then regarded as a research machine) purchased by the laboratory. Though, as Johnson later recalled, this did not prevent her from having to frequently cycle to the University of London computer centre at two o’clock in the morning to run her paper tape programmes that she had written through the more powerful computers there. The structure of lysozyme was determined by the start of 1965 and in November Phillips delivered a spectacular Friday Evening Discourse at the Royal Institution revealing publicly for the first time the structure. This was further explored at a Royal Society discussion meeting held at the Royal Institution in February 1966 where the paper by Johnson (who by now had been awarded her doctorate) made an especially memorable impact. In her paper she explained how the structure of lysozyme gave rise to its anti-microbial properties – this was the start of structural enzymology, a field in which she spent much of her research career.

Johnson then spent a year working in the Department of Biophysics at Yale University before rejoining Phillips who had moved, together with most of the lysozyme team, to Oxford as Professor of Molecular Biophysics, following Bragg’s retirement from the Royal Institution. She was initially a demonstrator in the Zoology Department and was later appointed to various lectureships before succeeding to Phillips’s chair when he retired in 1990, the same year that she was elected a Fellow of the Royal Society.

At some point Johnson had met the Professor of Theoretical Physics at Imperial College, Abdus Salam, fourteen years her senior who had been born in the Punjab. He belonged to a small Muslim sect, the Ahmadiyya, which in 1974 the government of Pakistan declared to be non-Muslim and deprived its members of civil rights. Salam was already married, with four children, but at the end of 1967 he and Johnson married and later they had two children. When Salam won the Nobel Prize in 1979, the Swedish authorities had the interesting protocol task of seating the two families. Salam was deeply interested in science in the developing world and in the careers of scientists from those countries, a cause to which Johnson was also fully committed, being elected an Associate Fellow of the Third World Academy of Sciences in 2000.

In 2003, the same year that she was created DBE, Johnson was appointed Director of Life Sciences at the Diamond Light Source built at Harwell. In large measure she was responsible for ensuring that a large part of this national facility was devoted to the bio-medical sciences and it continues to contribute significantly to them. She retired from her chair in 2007 and from Diamond the following year. Nevertheless, she remained scientifically active until a year or so before her death on 25 September 2012, the day before her 72nd birthday.

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