Dorothy Crowfoot Hodgkin: Biography, Contributions, Acknowledgments

Dorothy Crowfoot Hodgkin (1910-1994) was a British chemist, famous for her advances in the technique of x-ray crystallography that allowed her to decipher the molecular structure of important organic substances such as penicillin, insulin, and vitamin B 12.

She was awarded the 1964 Nobel Prize in Chemistry for this contribution to science, since from her findings researchers around the world were able to learn much more about the behavior and range of functions of the substances analyzed.

Dorothy Crowfoot Hodgkin. Source:

Other notable distinctions that the British scientist achieved were the Lomonosov Medal awarded by the Soviet Academy of Sciences, the Copley Medal, awarded by the Royal Society of London or the Austrian Decoration for Science and Art.

Article index

  • one


    • 1.1

      Early years

    • 1.2

      First contacts with chemistry

    • 1.3


  • two

    X-ray crystallography

    • 2.1

      First formal investigations

    • 2.2

      Structure of penicillin and vitamin B12

    • 23

      Structure of insulin

  • 3

    Nobel Prize in Chemistry

  • 4

    Academic work

  • 5

    His work around the world

  • 6

    Awards and honours

  • 7

    Personal life

    • 7.1


  • 8



Early years

Dorothy Mary Crowfoot was born on May 12, 1910 in Cairo, Egypt, a colony currently belonging to the British Empire. His parents were John Winter Crowfoot and Grace M. Hood.

The future scientist and her three sisters spent much of their childhood away from their parents, since with the start of World War I the girls were transferred to their grandparents’ house in England, while their parents remained in Africa for reasons of work.

At the time of Dorothy’s birth, her father worked in the Egyptian Education Service, from where he went to Sudan to serve as Deputy Director of Education. From there the couple moved to Israel where they both devoted themselves fully to archeology.

First contacts with chemistry

At the age of ten, the little girl was already conducting experiments in a makeshift laboratory in her grandparents ‘attic, analyzing crystals obtained from her occasional visits to her parents’ excavations in Africa.

During her adolescence she acquired her first knowledge about the technique that would make her world famous. All thanks to reading the book On the Nature of Things (1926) by the 1915 Nobel Prize winner in Physics and father of crystallography, William Henry Bragg.


Between 1921 and 1928 he attended Sir John Leman Secondary School in the town of Beccles, where he had to apply for special permission to attend Chemistry classes with the boys.

In 1928 she began studying Chemistry at Oxford University, an unusual decision at a time when women often chose a home life away from academia.

During her stay in this academic campus she attended a lecture by John Bernal (1901-1971) renowned crystallographer at the University of Cambridge and was so impressed by his crystallography technique that she decided to base her doctoral thesis on its study and application.

X-ray crystallography

Researchers of that time considered that the molecular structure of substances was linked to their functions, for this reason they had made considerable progress in the construction of models to understand their properties.

However, Crowfoot believed that finding new structures and correcting errors required seeing the molecule. To achieve this goal there was no better technique than x-ray crystallography.

This consisted of projecting a beam of x-rays through a substance in its crystallized version, dispersing a series of luminous points that were recorded on a photographic plate.

X-Ray Crystallography. Source: Deparment of Crystallography and Structual Biology

By analyzing the size of the light points, their location and separation from each other, the three-dimensional position of the atoms could be deduced with the use of mathematical calculations.

It was not an easy job, especially in a world without computers.

First formal investigations

Crowfoot spent two years in Bernal’s laboratory, located at the University of Cambridge, working on his doctoral thesis on the analysis of the structure of sterols through x-ray crystallography.

In 1934 he returned to the University of Oxford and began to seek funding to buy an x-ray machine and continue with this technique that he was so passionate about.

Structure of penicillin and vitamin B 12

Over time, Crowfoot earned her own fame as a leading crystallographer by discovering the architecture of substances that had never been elucidated before. In 1937 he revealed the structure of cholesterol and in 1945 that of penicillin.

Historians claim that because penicillin had a very complicated structure, Crowfoot had to make use of the first gigantic computers available at the time in order to complete his research.

Knowing the molecular structure would allow to synthesize and increase the production of this powerful antibiotic that since its discovery in 1928 by Alexander Fleming (1881-1955) had saved countless victims of infections.

His work with penicillin gave him good contacts with the pharmaceutical industry and access to crystals of vitamin B 12 , a substance that contributes to the formation of red blood cells and whose molecule is four times that of penicillin.

After nearly ten years of intensive research, Crowfoot presented the molecular model of vitamin B 12 in 1956 .

Penicillin molecular model

Source: Science Museum London / Science and Society Picture Library

Via Wikimedia Commons

Structure of insulin

In 1969, he completed his most complex research by developing the molecular model of insulin, a challenge that took him more than thirty years to overcome.

He had started his studies of the substance in 1938 when it was just beginning to be used for the treatment of diabetes and its structure or all its functions were not yet known.

At one point in his research, he managed to obtain a first molecular image that allowed him to publish his first solo article, in which he affirmed his hope of unraveling its structure, which was almost 50 times larger than that of penicillin.

To achieve this, she eventually created a department made up of programmers and mathematicians to work on the calculations that ultimately helped her achieve the elusive structure of insulin.

Nobel Prize in Chemistry

In 1964 all his effort was highly recognized with the Nobel Prize in Chemistry “for determining the structures of important biochemical substances by means of x-ray techniques.”

Crowfoot was the first British woman to win a Nobel Prize and the third woman in history to win the Chemistry section, only after the Polish Marie Curie (1867-1934) and her daughter, the French Irene Joliot-Curie (1897-1956 )

Academic work

Since 1936, the University of Oxford appointed her as its first chemist researcher and tutor. His success in the field of x-ray crystallography attracted numerous students to his laboratory. It is said that he even taught the future British Prime Minister, Margaret Thatcher.

In 1946 he took an active part in the meetings prior to the founding of the International Union of Crystallography and frequently received visits to his laboratory from scientists from various parts of the world, including the former Soviet Union and China.

In 1960 she also served as a research professor at the Royal Wolfson Society, in Oxford from where she retired in 1970 to take up the rectory of the University of Bristol.

His work around the world

Her experience made her a person in high demand by other laboratories and international organizations that wanted to know her knowledge firsthand.

He traveled lecturing, reporting on his findings, and even serving as a pacifist by openly rejecting the Vietnam War and taking part in the Pungash World Affairs and Science Conferences, a series of meetings between scientists who rejected the construction of weapons of mass destruction.

Awards and honours

In addition to the Nobel Prize, Crowfoot earned other accolades throughout his career. Here are some of them:

– 1947. Member of the Royal Society of London.

– 1958. Foreign Honorary Member of the American Academy of Arts and Sciences.

– 1966. National Honorary Member Iota Sigma Pi.

– 1970. Member of the European Molecular Biology Organization.

– 1982. Lomonosov Medal awarded by the Soviet Academy of Sciences.

– 1982. Asteroid 5422 was identified with the name Hodgkin in his honor.

– 1983. Austrian Decoration for Science and Art.

– 1987. Lenin Peace Prize.

– 2015. Cita Award for the discovery of the structure of penicillin.

– 2016. Copley Medal, awarded by the Royal Society of London.

– She was also appointed a foreign member of the Academy of Sciences of the Soviet Union.

– It has been commemorated on British postage stamps twice.

– A scholarship awarded by the Royal Society of London was named in his honor.

– Several offices and buildings located in government and university spaces bear his name.

– In 2012, during Queen Elizabeth II’s Diamond Jubilee, Crowfoot was named among those whose actions had a significant impact on the monarch’s period

– The University of Oxford annually organizes the International Women’s Festival with a conference of leading scientists who, in each edition, analyze aspects related to Crowfoot’s research.

Personal life

In 1934 at just 24 years old, Crowfoot began to suffer from painful inflammations in her hands and was diagnosed with rheumatoid arthritis. This degenerative disease that eventually led her to have to use a wheelchair, did not divert her from her scientific projects and demonstrated her mettle and perseverance in the face of adversity.

Despite her illness and the absorbing nature of her work, the scientist made room in her life to establish a family. In 1937 she married the historian Thomas Hodgkin with whom she had three children: Luke, Elizabeth and Toby.

Years after his marriage, he began to sign his publications with the name Dorothy Crowfoot Hodgkin.


The Nobel Prize organization described Crowfoot as a woman with great intuition, imagination and perseverance, characteristics that certainly accompanied her throughout her life and that helped her achieve all her scientific purposes.

He died of a stroke on July 29, 1994 in Shiptons-on-Stour, United Kingdom, after a lifetime devoted to science and the discovery of structures that stopped the advance of disease and extended the average life of the human being in full twentieth century.


  1. The Nobel Prize Organization. (1964) Dorothy Crowfoot. Taken from
  2. Georgina Ferry. (2019). Dorothy Dodgkin. Taken from
  3. Science History Institute. (2019). Dorothy Crowfoot Hodgkin. Taken from
  4. San Diego Super Computer Center. (2019). Dorothy Crowfoot Hodgkin, OM. A founder of protein crystallography. Taken from
  5. International Union of Crystallography. (2019). Dorothy Crowfoot Hodgkin. Taken from

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