by Ryan Hoffman

Dorothy Crowfoot Hodgkin was born in 1910, in Cairo, Egypt. Her mother, Molly, and father, John Crowfoot, had met in Lincoln, England, and had moved to North Africa owing to John's participation in the British administration of Egypt as a civil servant in the Department of Education. Following the out­break of World War I, Hodgkin was relocated to England. She spent most of her childhood in Norfolk, where she was permit­ted to join the boys in chemistry class—an unusual exception, likely facilitated by Criss Deeley, a female teacher of chemistry, mathematics and needlework at her school. Hodgkin’s family supported her early interest in chemistry with a small lab space in the attic of their Norfolk residence, and with two published versions of a lecture series for children, delivered by William Bragg in 1923 and 1925, that addressed the use of X-rays to study the properties of matter. She thus became enam­ored with X-ray analysis well before her sixteenth birthday.

Molly and John shared an interest in archeology that they instilled in their children; they even participated in archeologi­cal digs. For her university education Hodgkin attended Oxford from 1928-1932, nurturing her early interests through the chemical analysis of archeologically significant mosaic tiles. She was impressed with an Oxford lecture from the crystallogra­pher J. D. Bernal, and converged on the applications of crystal­lography as her major scientific interest. She spent 1932-1934 at Cambridge studying with Bernal; the ensuing relationship would span decades. The two would make important contri­butions to the early field of protein crystallography, although the bulk of their collaborations were centered on the structure determinations of small organic molecules, especially sterols. In 1934, they co-published the seminal observation that an X-ray diffraction pattern could only be obtained from hydrated protein crystals.

In 1937, Hodgkin met and married Thomas Lionel Hodgkin. Thomas had served in the (British mandate) Palestine civil service, and like Hodgkin’s parents, he had become disillu­sioned with British Imperialism. The Hodgkins would remain closely associated with other British intellectuals interest­ed in anti-imperialism, racial tolerance, and world peace. Hodgkin's unapologetically left-wing views and association with Communist Party members (including her husband and Bernal) prevented her from receiving a U.S. Visa from 1953- 1990. Luckily she had numerous productive visits with Linus Pauling and other American leaders in protein crystallography prior to this clampdown.

Hodgkin was the first woman at Oxford to receive paid mater­nity leave surrounding the birth of her first child in 1938, in fact, she was the first Oxford Fellow to give birth while in her post. At the time, even marriage was unusual for a female Fellow. She continued in her quietly iconoclastic fashion, addressing the Royal Society that year, while visibly pregnant, and under the appellation “Miss. Dorothy Crowfoot.” Throughout World War II, she grew her family while consolidating her status as a crystallographer with her discovery of the structure of penicil­lin, a result of “national interest” during the war, generating many accolades. These included nomination for the Royal Society in 1947, the third woman to be nominated since their eligibility was established in 1922. Oxford itself would be slower to celebrate her accomplishments with a promotion to Reader in X-Ray Crystallography coming several years later in 1955.

Hodgkin worked on the insulin structure for over 30 years, eventually publishing the initial result in 1969. This happened shortly after she was awarded the Nobel Prize in Chemistry (1964) for discovering the structure of vitamin B-12. Insulin would not be the first atomic-precision protein structure despite Hodgkin and Bernal's long-standing priority in the reporting of single-crystal diffraction patterns. Max Perutz and John Kendrew received the 1962 Nobel Prize in Chemistry for their structures of myoglobin and hemoglobin. Perutz empha­sized Hodgkin’s contributions to the field that preceded their major accomplishments. Similarly, in a single exchange with Rosalind Franklin, Hodgkin explained how, of the three space groups that Franklin had considered to be consistent with her DNA diffraction photograph, only one was consistent with the chiral nature of the deoxyribose.

Hodgkin had developed chronic rheumatoid arthritis following an infection she contracted after the birth of her first child. This affected her for the rest of her life, leaving her hands swollen and distorted, but did not stop her from becom­ing one of the most skilled crystallographers of her time.

Following the Nobel Prize, Hodgkin rapidly accumulated addi­tional honors as she continued to advance scientific diplo­macy. She was appointed Chancellor of the University of Bristol in 1970. In 1972, she took office as the President of the International Union of Crystallography. Although she was the third female Laureate in Chemistry, Hodgkin is not a house­hold name, perhaps due to the public’s lack of familiarity with crystallography. Perhaps if she were celebrated more visibly, it would advance popular appreciation of structural biology.

References

Georgina Ferry, Dorothy Hodgkin: a life. Cold Spring Harbor Laboratory Press (2000) http://www.nobelprize.org/nobel_ prizes/chemistry/laureates/1964/hodgkin-bio.html