Hodgkin obtained her first insulin sample and began pioneering X-ray diffraction studies of insulin crystals.
In early 1934, as a young researcher at Cambridge, Dorothy Hodgkin received her first sample of crystalline insulin from biochemist Robert Robinson and began taking some of the earliest X-ray diffraction photographs of the protein. This marked the beginning of what would become a 35-year quest to fully determine insulin's three-dimensional structure.
At the time, insulin's chemical composition was known, but its complex three-dimensional folding remained a total mystery. X-ray crystallography of proteins was itself a nascent and highly experimental technique, requiring painstaking preparation of pure crystals and laborious manual calculation of diffraction patterns—decades before computers made such analysis feasible.
Hodgkin's early insulin photographs demonstrated that the protein did indeed produce discernible diffraction patterns, proving that its atomic structure could, in principle, be solved by X-ray methods. This was a foundational moment not just for her own career but for the emerging field of protein crystallography as a whole.
The insulin problem would occupy Hodgkin on and off for the rest of her working life, symbolizing both the promise and the immense technical challenge of structural biology in the mid-twentieth century. Her patience and methodological innovation in this early period set the stage for one of the most celebrated achievements in the history of biochemistry.