Lord Phillips of Ellesmere KBE FRS in interview with Dr Max Blythe: Interview 3

• Main Authors: Phillips, David, Blythe, Max
• Other Authors: Oxford Brookes University, The Royal College of Physicians
• Format: Moving Image (Video)
• Language: English
• Published: Oxford Brookes University 2017
• Subjects: Biophysics; Research; Protein crystallography (x-ray); Blythe; Canada; Perutz; Sperm whale
• Online Access: https://doi.org/10.24384/000094; https://radar.brookes.ac.uk/radar/file/a18fa59a-58d2-487f-b608-67c07544b453/1/OB_PHILLIPS-BLYTHE_INT3_29-04-96_4x3_133_SD_MX1-1631809.mp4; https://radar.brookes.ac.uk/radar/file/a18fa59a-58d2-487f-b608-67c07544b453/1/Phillips_3.pdf

Much of the conversation of this third interview with Lord Phillips of Ellesmere KBE FRS reflects the remarkable advances of x-ray crystallography in the 1950s. The field was expanding dramatically with innovative groups and publications springing up widely. In a number of laboratories the crystallographic investigation of protein structure was gathering momentum, but not the National Research Laboratories in Ottawa, Canada, where he moved to a post-doctoral fellowship in 1951. Here work on the structure of polymorphic variants of acridines begun in Cardiff continued, with important refinements of technique and critical advances in the processing of three dimensional data, with assistance in computer programming from Farid Ahmed who had trained with Cruikshank in Leeds, collaboration with whom led to direct three dimensional analysis, a massive advance on the two dimensional projections on which earlier work had been based. A number of technical problems associated with the visual estimation of diffraction patterns were also solved geometrically, resulting in a major publication of the time. Opportunities for travel and communication with other laboratories further extended interest in technical advances, especially in diffractometer design, which is discussed. The Canada years, 1951-55, were critical foundation years in which innovative research and growing technical achievements provided a first degree of international recognition. They were years, too, important for their social impact and a broadening of leisure outlook. But in the end it was not difficult to respond to an invitation to return to a post at London's Royal Institution. The future in Canada had no long-term attractions and an opportunity to work with pioneering crystallographer Sir Lawrence Bragg was grasped, an opportunity to work in protein crystallography. Recalling this transfer to London in some detail, Lord Phillips sets the scene at the Royal Institution in 1956, the character of the establishment recently under Bragg's direction, and the personnel being recruited to develop crystallography there. There is also reference to Bragg's former Cambridge colleagues Max Perutz and John Kendrew and the extent to which they were to be involved. Collaborative research with John Kendrew is the main subject of the interview's remaining footage, research on the structure of myoglobin. Kendrew's team at Cambridge was already underway with studies of sperm whale myoglobin, while at the Royal Institution crystallographic studies of seal myoglobin became the focus, a complex challenge for a new unit, but one quickly harnessing innovative developments, many of which are colourfully recounted, with clear reference to the various innovators. The emergence of the detailed structure of myoglobin brings the interview to its summit, although a number of valuable recollections relating to Perutz and Kendrew follow, also reference to involvement with the International Science Exhibition at Brussels in 1960. A transfer to studies of the enzyme lysozyme is the subject of Interview 4.