Robert Huber's path to a Nobel chemistry prize wasn't immediately clear, as his secondary school in Munich focused on Latin and Greek. But his early fascination with the chemistry of minerals, born on walks in the nearby mountains, soon asserted itself. Studying chemistry at the Technical University of Munich in the 1950s, he delved into the newly developing field of crystallography.

Huber's experimental drive was the perfect complement to the theoretical focus of his doctoral mentor, Walter Hoppe. Huber elaborated on Hoppe's proposed method for molecular crystallography by experimentally determining crystal structures using molecular fragments. His dissertation elucidating the insect metamorphosis hormone, ecdysone, boosted his reputation. Switching to protein analysis, he deciphered the crystal structure of the insect protein erythrocruorin, a blood protein similar to mammalian proteins. Prestigious offers followed, and he began a 30-year career as director of structural research at the Max Planck Institute of Biochemistry in Martinsried.

Taking advantage of refined crystallography methods and instrumentation, Huber teamed up with his former PhD student Johann Deisenhofer and colleague Hartmut Michel to tackle one of the most important molecular structural targets in biology — the photosynthetic reaction centre, which converts solar rays into electrical energy. Determining its structure, the first one determined for a crystalline membrane protein, earned them the 1988 Nobel Prize in Chemistry. This didn't significantly affect Huber's career, but it did help him attract even better students.

After retiring at 68, as dictated by German law, Huber recently accepted a part-time position to help form an interdisciplinary chemical-biology initiative: a programme linking the schools of chemistry and biosciences at Cardiff University in Wales. He will teach classes as well as advise on strategic investments and recruitment.

“He's helped us find a focus — the structural basis for drug development — to build our activities around,” says Adrian Harwood, a biosciences professor at Cardiff. He adds that Huber's excellent track record in helping develop structural-biology programmes at other universities will catalyse the new initiative.

Huber plans to continue promoting the field by energizing students. “I saw structural biology being born, and now I see it almost matured, providing the basis for our understanding of biology and medicine,” he says. (see CV)