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Crystallography of biomolecules

revealing the workings of nature’s smallest machines South East,

A collection of red, black, blue and white balls arranged on a wire frame.
Vitamin B12 crystal structure model, 1957-59. Science Museum/ Science 7 Society Picture Library

Dorothy Crowfoot Hodgkin (1910-94) advanced the methods used to study atoms and molecules in living things, which are critical for understanding how they work. 

She had been fascinated by crystals from an early age, and having graduated from the University of Oxford began working on X-ray crystallography - a technique used to identify the structure of molecules - and was a pioneer in extending its use to biomolecules. 

In 1946 she had her first major success when she uncovered the molecular structure of the antibiotic penicillin. However, it was revealing the structure of the complex vitamin B12 ten years later that brought her the greatest recognition. She also went on to map the structure of insulin. In 1964 she won the Nobel Prize in Chemistry, particularly ‘for her determinations by X-ray techniques of the structures of important biochemical substances’. 

This effort to reveal protein structures at the atomic level enhances our understanding of how they work, such as the way enzymes speed reactions. Armed with this information we can design novel drugs that target a particular protein, or rationally engineer an enzyme for industrial use.

Science Museum

Chemistry, Biology,
South East
University of Oxford
Key Individuals
Dorothy Crowfoot Hodgkin,