A Founder of Protein Crystallography
Scientific biographers do not, in general, find much correlation between good character and great science. There are a few exceptions. Historians have unanimously agreed, for example, that Charles Darwin was a particularly admirable, even lovable, figure: a collegial scientist, devoted father, faithful supporter of young colleagues, sincere, honest, and without personal enemies.
The Darwin of our age is certainly Dorothy Crowfoot Hodgkin. In the words of colleague Max Perutz (Nobelist for his solution of the hemoglobin molecule), she was "a great chemist, a saintly, gentle and tolerant lover of people, and a devoted protagonist of peace." In a short space it is impossible to discuss both the significance of her science and the scope of her tireless activity for world peace.
Concentrating first on her contributions to science, she is known as a founder of the science of protein crystallography. She and her mentor, J.D. Bernal, were the first to successfully apply X-ray diffraction to crystals of biological substances, beginning with pepsin in 1934. Hodgkin's contributions to crystallography included solutions of the structures of cholesterol, lactoglobulin, ferritin, tobacco mosaic virus, penicillin, vitamin B-12, and insulin (a solution on which she worked for 34 years), as well as the development of methods for indexing and processing X-ray intensities. After the work with Bernal, she established her own laboratory at Oxford, described in the memoirs of her many students as an unfailingly joyful and productive environment.*
The challenges were always huge, as every new technique seemed to reach limits that constrained the size of protein that could be successfully solved, and each protein tackled presented special problems of its own. Hodgkin was elected a Fellow of the Royal Society in 1947 after publishing the structure of penicillin and was awarded the Nobel Prize in Chemistry in 1964 for her solution of vitamin B-12. The solution of the insulin structure came in 1969, after many years of struggle. Hodgkin and her collaborators produced a more refined solution in 1988, one that took full advantage of computational techniques that can now reduce the time for protein solutions from years to months or weeks.
Hodgkin was the first of four daughters of John and Grace Crowfoot. Her father was an archaeologist working for the Ministry of Education in Cairo and her mother, an accomplished artist, was an expert on Coptic textiles. Dorothy married Thomas Hodgkin, an expert in African Studies, in 1937, and they had three children.
Hodgkin's role in the arena of science policy and international relations was a constant complement to her own scientific work. The entire family distinguished itself over more than three decades by working in the public arena for the cause of world peace. She belonged to many international peace organizations and, owing to Cold War restrictions, was not permitted to obtain a U.S. visa until 1990. Although she was over 80 and extremely crippled by rheumatoid arthritis, she lost no time in making a grand tour of U.S. institutions to discuss insulin, the history of crystallography, and its future. Her talks drew standing-room-only crowds at every stop. She suffered a stroke and died in 1994.
* Guy Dodson, Jenny P. Glusker, and David Sayre (Eds.), 1981: Structural studies on molecules of biological interest: A volume in honour of Professor Dorothy Hodgkin. (Oxford: The Clarendon Press).