Max Perutz

Max Perutz was an Austrian-born British molecular biologist who used X-ray crystallography to determine the structure of hemoglobin and explain how it carries oxygen.

John Kendrew: A British molecular biologist who determined the three-dimensional structure of myoglobin by X-ray crystallography. Perutz’s colleague at Cambridge, Kendrew solved the first protein structure at atomic resolution.
Hemoglobin: A tetrameric protein in red blood cells that transports oxygen and helps carry carbon dioxide. Its atomic structure was the central object of Perutz’s crystallographic research.
Vienna: The capital of Austria and a major European center of science, music, and culture. Perutz was born and educated in Vienna before leaving Austria for Britain.
1953 protein structure paper by Perutz: A paper by Max Perutz reporting X-ray diffraction evidence about the structure of hemoglobin. This work showed that protein crystals could reveal organized molecular structure, despite limited diffraction data.
Francis Crick: A British molecular biologist who co-discovered the structure of DNA and helped establish molecular biology. Crick and Perutz worked in the same Cambridge community that made molecular structure a central biological question.
X-ray crystallography: A method that infers atomic arrangements from the diffraction of X-rays by crystals. Perutz adapted this method to extract structural information from hemoglobin crystals.
University of Cambridge: A public research university in Cambridge, England, founded in 1209. Perutz joined Cambridge in 1936 and built his long-term research career there.
Nobel Prize in Chemistry: An annual international award recognizing outstanding achievements in chemistry. Perutz shared the 1962 prize with John Kendrew for studies of globular proteins.
Dorothy Hodgkin: A British chemist who used X-ray crystallography to determine the structures of complex biological molecules. Her crystallographic work helped establish methods and standards that Perutz’s protein studies advanced.
Molecular replacement: A crystallographic method that uses a known molecular structure to help solve a new crystal structure. Perutz’s phase-solving work helped develop approaches that made protein diffraction data interpretable.

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