Crystallography

Rosalind Franklin's X-ray diffraction image of DNA—nicknamed "Photo 51"—was shown to Watson and Crick without her permission, leading directly to their double helix model in 1953. This single crystallographic image, showing the telltale X-shaped pattern of a helix, became one of the most consequential photographs in scientific history. Franklin died before the Nobel Prize was awarded, highlighting both crystallography's revolutionary power and the complex human dynamics behind scientific breakthroughs.

Traditional crystallography required perfect crystal lattices, but many crucial biological molecules—like membrane proteins that comprise 60% of drug targets—refused to crystallize properly for decades. The 2017 Nobel Prize in Chemistry recognized cryo-electron microscopy as crystallography's rebellious sibling, allowing scientists to visualize molecules frozen in their natural, messy states. This breakthrough means we can now design drugs for previously "invisible" targets, including receptors involved in pain, addiction, and neurological diseases.

Dorothy Crowfoot Hodgkin began her X-ray crystallography work on insulin in 1934 but didn't solve its complete structure until 1969—a testament to both the technique's difficulty and her persistence. Before modern computers, crystallographers manually calculated thousands of equations to interpret diffraction patterns, sometimes taking years per molecule. Today's automated systems can solve crystal structures in hours, but Hodgkin's insulin work laid the foundation for understanding how protein shape determines function, revolutionizing diabetes treatment and protein engineering.

In 1982, Dan Shechtman observed a diffraction pattern that "couldn't exist" according to crystallographic law—a five-fold symmetry that violated the fundamental rules of how atoms pack together. He was ridiculed and asked to leave his research group, yet quasicrystals are now found in everything from non-stick frying pans to LED lights. This discovery, which won the 2011 Nobel Prize, forced crystallographers to rewrite their textbooks and proved that nature is more creatively disordered than we assumed.

Every semiconductor chip in your devices relies on crystallographic perfection—silicon crystals grown so flawlessly that impurities are limited to less than one atom per billion. Crystallographers map these atomic arrangements to engineer precise electronic properties, determining everything from processor speed to solar cell efficiency. When your phone's screen cracks, you're literally seeing crystal planes fracturing along their weakest atomic bonds—a visible reminder that crystallography isn't just academic, it's in your pocket.

Since 1971, the Protein Data Bank has archived every solved molecular structure, growing from 7 entries to over 200,000 today—a library of life's machinery freely available to anyone. Drug designers browse this database like architects consulting blueprints, finding binding pockets in disease proteins or comparing enzyme shapes across species. This open-access treasure, built primarily through crystallography, has democratized molecular science, allowing a researcher in Nairobi and a startup in Singapore to design molecules with the same structural intelligence as major pharmaceutical companies.