Biography

Wolfgang Baumeister studied biology, chemistry and physics at the Universities of Muenster and Bonn, Germany, and he obtained his Ph.D. from the University of Düsseldorf in 1973. He spent time at the Cavendish Laboratory in Cambridge, England, and in 1978 became lecturer in biophysics. In 1983 he moved to the Max Planck Institute for Biochemistry in Martinsried, Germany, where he became director in 1988 and head of the Department of Structural Biology.

He is also an Honorary Professor of Physics at the Technical University of Munich. Baumeister is the recipient of numerous prizes including the Otto Warburg Medal, Schleiden-Medal, Louis-Jeantet Prize for Medicine, Stein and Moore Award and Harvey Prize in Science and Technology. He is a member of several academies including the American Academy of Arts & Sciences.

Baumeister’s research interests are in the field of cellular protein quality control. He has discovered and characterized several novel complexes which play key roles in protein folding and degradation and he made seminal contributions to our understanding of the structure and function of the proteasome. Moreover, he has pioneered the development of cryoelectron tomography, an emerging imaging technique with unique potential for molecular cell biology.
 

Wolfgang Baumeister, Ph.D.

Director of the Department of Molecular Structural Biology
Max Planck Institute for Biochemistry

wwwex.biochem.mpg.de/baumeister/

Mapping Molecular Landscapes inside Cells by Cryoelectron Tomography

Abstract:
With the advent of computer-controlled electron microscopes and the automation of data acquisition, it became possible to obtain molecular-resolution (2-4 nm) tomograms of structures as large as organelles or whole cells. Noninvasive three-dimensional (3-D) imaging of vitrified cells is where cryoelectron tomography promises to make unique contributions by closing the gap between the cellular and the molecular worlds. The emerging picture of the cell is one of a giant and highly dynamic supramolecular assembly, hitherto a largely uncharted territory. Tomograms of cells at molecular resolution are essentially 3-D images of the cell’s entire proteome, and they reveal the spatial relationships of macromolecules in the cytoplasm, the “interactome”. To exploit the imposing amount of information contained in a cellular tomogram, sophisticated pattern recognition techniques must be used that are capable of detecting and identifying molecules in tomograms with a low signal-to-noise ratio through their structural signature. The ultimate goal is to obtain, through a combined proteomics-electron tomography approach, a comprehensive 3-D molecular atlas of cells and organelles and to reveal the principles of supramolecular organization that provide the basis for higher cellular functions.