Carl Hermann Medal awarded to Udo Heinemann

At the annual meeting of the German Society for Crystallography (DGK) in Hanover, Professor Udo Heinemann will likely stand out as an odd ball. “Most of the scientists attending are materials researchers, focused on optimizing solar cells or semiconductors,” says the structural biologist. In contrast, Heinemann has spent over 25 years leading a research group at the Max Delbrück Center – conducting biomedical research.

Nevertheless, the 71-year-old will receive the society’s highest honor during the conference’s opening ceremony on March 10: the Carl Hermann Medal. According to the DGK, the award recognizes “the scientific lifetime achievements of outstanding researchers in the field of crystallography.”

X-rays and crystallized proteins

“I am, of course, extremely grateful for this recognition and appreciation of my work – but my success would have been impossible without my colleagues in the lab, to whom I owe my deepest gratitude,” says Heinemann, who continues to serve at the Max Delbrück Center as an ombudsperson for good scientific practice after retiring. “When I look at past recipients of this award, I see a list filled with colleagues who are highly influential in their fields.”

I am, of course, extremely grateful for this recognition and appreciation of my work – but my success would have been impossible without my colleagues in the lab, to whom I owe my deepest gratitude.

That a scientist focused on biological structures is now among the honorees – who, so far, have been exclusively men – is no accident. “For a long time, the only way to determine the spatial structures of proteins, nucleic acids, or other cellular components was by isolating, crystallizing, and exposing them to x-rays,” Heinemann explains.

The x-rays created a diffraction pattern in the crystals, which computers analyzed to deduce the three-dimensional shape of the molecules. This method even made it possible to visualize individual atoms and the bonds between them.

Experiments as a foundation for AI-based software

Throughout his career, Heinemann studied how proteins attach to DNA and the resulting effect. He also sought to understand transport processes within cells. “Using crystallography, we formulated hypotheses about these mechanisms and then validated them through other research approaches,” he says.

Today, researchers increasingly answer these questions through cryo-electron microscopy or artificial intelligence tools like the AlphaFold software – eliminating the need for physical experiments. “However, these AI predictions are only made possible because of the experimental data we generated,” Heinemann points out. “They work because of the knowledge we painstakingly uncovered in the lab.”

Still, AI alone cannot always detect certain molecular behaviors. One of Heinemann’s favorite projects was a structural analysis he conducted about ten years ago with Erich Wanker’s research group at the Max Delbrück Center. They studied the protein p97, which extracts energy from ATP molecules in human cells to break down larger molecules.

New drugs thanks to crystallography

“When p97 bound to another specific class of proteins, its structure changed in a completely unexpected way – something AI could never have predicted,” Heinemann recalls. “Hopefully, younger researchers will one day uncover the full significance of this surprising transformation.”

Even today, crystallography provides the most precise insights into molecular structures. “This is especially important for drug development – helping scientists understand how a pharmaceutical molecule binds to its target structures,” Heinemann explains. Crystallography plays a key role in accelerating the development of new medications, making them available to patients more quickly.

Text: Anke Brodmerkel

Further information

• Portrait of Udo Heinemann