In 1945 he approachedMax Perutz in theCavendish Laboratory inCambridge.Joseph Barcroft, a respiratory physiologist, suggested he might make a comparative protein crystallographic study of adult and foetal sheep haemoglobin, and he started that work.
In 1947 he became a Fellow ofPeterhouse; and theMedical Research Council (MRC) agreed to create a research unit for the study of the molecular structure of biological systems, under the direction of SirLawrence Bragg.[9] In 1954 he became a Reader at the Davy-Faraday Laboratory of theRoyal Institution inLondon.
In 1947 the MRC agreed to make a research unit for the Study of the Molecular Structure of Biological Systems. The original studies were on the structure of sheep haemoglobin, but when this work had progressed as far as was possible using the resources then available, Kendrew embarked on the study ofmyoglobin, a molecule only a quarter the size of the haemoglobin molecule. His initial source of raw material washorse heart, but the crystals thus obtained were too small for X-ray analysis. Kendrew realized that the oxygen-conserving tissue ofdiving mammals could offer a better prospect, and a chance encounter led to his acquiring a large chunk ofwhale meat from Peru. Whale myoglobin did give large crystals with clean X-ray diffraction patterns.[10] However, the problem still remained insurmountable, until in 1953Max Perutz discovered that thephase problem in analysis of the diffraction patterns could be solved bymultiple isomorphous replacement — comparison of patterns from several crystals; one from the native protein, and others that had been soaked in solutions of heavy metals and had metal ions introduced in different well-defined positions. An electron density map at 6angstrom (0.6nanometre) resolution was obtained by 1957, and by 1959 an atomic model could be built at 2 angstrom (0.2 nm) resolution.[11]
In 1963, Kendrew became one of the founders of theEuropean Molecular Biology Organization; he also founded theJournal of Molecular Biology and was for many years its editor-in-chief. He became Fellow of the American Society of Biological Chemists in 1967 and honorary member of the International Academy of Science, Munich. In 1974, he succeeded in persuading governments to establish theEuropean Molecular Biology Laboratory (EMBL) inHeidelberg and became its first director. He was knighted in 1974.[3] From 1974 to 1979, he was a Trustee of theBritish Museum, and from 1974 to 1988 he was successively Secretary General, Vice-President, and President of theInternational Council of Scientific Unions.
After his retirement from EMBL, Kendrew became President ofSt John's College at theUniversity of Oxford, a post he held from 1981 to 1987. In his will, he designated his bequest to St John's College for studentships in science and in music, for students from developing countries. TheKendrew Quadrangle at St John's College in Oxford, officially opened on 16 October 2010, is named after him.[12]
Kendrew was married to the former Elizabeth Jarvie (née Gorvin) from 1948 to 1956. Their marriage ended in divorce. Kendrew was subsequently partners with the artist Ruth Harris.[3] He had no surviving children.[13]
Kendrew, JC (July 1959). "Structure and function in myoglobin and other proteins".Federation Proceedings.18 (2, Part 1):740–51.ISSN0014-9446.PMID13672267.
John Finch; 'A Nobel Fellow on Every Floor', Medical Research Council 2008, 381 pp,ISBN978-1-84046-940-0; this book is all about the MRC Laboratory of Molecular Biology, Cambridge.
