Prof. Robert Huber was born in 1937 in Munich. He completed his Ph.D.  at Technical University Munich (TUM). Since 1972, he has been a member of the Max-Planck-Gesellschaft and Director at the Max Planck Institute for Biochemistry until his retirement in 2005. He has recently taken up a post at the Cardiff University and will spearhead the development of Structural Biology at the university on a part time basis. Huber has made major contributions to the understanding of the structure and function of biological macromolecules. He has studied proteases and their natural and synthetic inhibitors, metalloenzymes (iron, nickel, molybdenum, copper), proteins of the immune system (antibodies and antibody receptors), protein hormones and their receptors, protein kinases,  enzymes of amino acid biosynthesis,  enzymes of cofactor and vitamin biosynthesis and proteins of energy and electron transfer. In addition, he has contributed to the development of instruments for data collection and to methods in protein crystallography, particularly Patterson methods, graphic methods, and refinement, to the use of electron rich metal clusters, and most recently to the methods and instruments for crystal improvement.  In 1988 he received the Nobel Prize in Chemistry jointly with Johann Deisenhofer and Harmut Michel. The trios were recognized for their work in first crystallizing an intramembrane protein important in photosynthesis in purple bacteria, and subsequently applying X-ray crystallography to elucidate the protein's structure. The information provided the first insight into the structural bodies that performed the integral function of photosynthesis. This insight could be translated to understand the more complex analogue of photosynthesis in cyanobacteria which is essentially the same as that in chloroplasts of higher plants.