John Kendrew attends Clifton College in Bristol.
John Kendrew attends as a Major Scholar Trinity College, where he graduates in chemistry.
John Kendrew is born in Oxford, son of Wilford George Kendrew, Reader in Climatology in the University of Oxford and Evelyn May Graham Sandburg, art historian.
John Kendrew leaves Cambridge for the post of Director-general of the European Molecular Biology Laboratory in Heidelberg. In 1974 Kendrew is also knighted.
John Kendrew dies in Cambridge at the age of 80.
John Kendrew earns his Ph.D. with a research on the protein myoglobin at Cavendish Laboratory. There, he collaborates with Max Perutz in studying the structure of haemoglobin, under the direction of Sir Lawrence Bragg.
In 1981, John Kendrew becomes President of St John's College at Oxford University.
John Kendrew is Department Chairman of the Medical Research Council Laboratory for Molecular Biology.
John Kendrew becomes Member of the Air Ministry Research Establishment (later Telecommunication Research Establishment), working on the application of airborne radar to the war effort.
John Kendrew attends Dragon School at Oxford.
John Kendrew spends the first few months of World War II researching on reaction kinetics in the Department of Physical Chemistry at Cambridge under the supervision of Dr. E.A. Moelwyn-Hughes.
John Kendrew receives one half of the Nobel Prize for Chemistry along with Max F. Perutz "for their studies of the structures of globular proteins". Kendrew is credited with pioneering the use of X-ray crystallography to determine the complex structure of proteins. His work helped to set the stage for the development of molecular biology.
In 1947 John Kendrew becomes a Fellow of Peterhouse in Cambridge, in 1960 he becomes also Fellow of the Royal Society , and an honorary member of the American Society of Biological Chemists in 1962.
John Kendrew starts working in operational research at the Royal Air Force headquarters, holding the honorary rank of Wing Commander R.A.F. He leads his researches first in England, then in the Middle East, and finally in Southeast Asia. During those years Kendrew meets J. D. Bernal and Linus Pauling the combined influence of which persuades him to pursue his doctorate in biology instead of chemistry.
In 1953, Perutz finds a way to define heavy atoms' positions in the haemoglobin crystal (method, known as isomorphic replacement). Kendrew applies it to the simpler molecule myoglobin, succeeding by 1957 in unravelling the first protein structure. It is only in 1959-1960 that Kendrew and his group achieve a very high photographic resolution: most of the individual atoms are now visible.