The International Max Planck Research School for Chemical and Molecular Biology (IMPRS-CMB) is a collaboration between the Max Planck Institute of Molecular Physiology and three universities, the Technical University Dortmund (TU Dortmund), the Ruhr University Bochum (RUB) and the University of Duisburg-Essen (DUE).

All four institutes are located in the Ruhr Metropolitan Area of Germany, an extremely vibrant and culturally interconnected region. The same spirit is reflected in the science of our program: research groups, with different and often complementary approaches, combine their efforts to study at the molecular level basic cell physiology.

Below you can find all the research groups that are part of IMPRS-CMB, in alphabetical order. You can also search groups by name, topic or technique.

Read about OUR SCIENCE by visiting the webpages of our Faculty Members.


Prof. Dr. Stefan Raunser

Current Position: Director, Department of Structural Biochemistry, Max Planck Institute of Molecular Phyisiology, Dortmund; Adjunct Professor, Faculty of Chemistry and Chemical Biology, Technical University Dortmund and Honorary Professor, Centre for Molecular Biotechnology, University Duisburg-Essen
01/2014-06/2014: Einstein-Professor for Membrane Biochemistry (W3) at Freie Universität, Berlin
2008-2013: Independent Group Leader at the Max Planck Institute of Molecular Phyisiology, Dortmund

2005-2008: Postdoc in the laboratory of Dr. T. Walz, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA, USA
2001-2004: PhD in the laboratory of Dr. W. Kühlbrandt, MPI of Biophysics, Frankfurt
1995-2000: Studies of Biology and Chemistry at the University of Mainz and at the Nottingham Trent University, UK

Research Interest
The research of our group focuses on structural and functional studies of macromolecular complexes. In particular, we focus on sterol-sensing membrane proteins that are involved in cholesterol homeostasis, transport and synthesis. Our group uses electron crystallography and X-ray crystallography, respectively, to determine the structure of the respective membrane proteins in their near-to-native lipidic environment and at high resolution. Besides structural studies, we are exploring the function of these proteins in vivo and in vitro by biochemical and functional studies as well as by cellular assays.
Another major interest of our group is to understand the function and structural organization of bacterial toxin complexes that permeate the membrane and translocate actin-attacking enzymes into the target cell. We use a hybrid approach, including biochemical reconstitution, structural analysis by single particle cryo-EM and X-ray crystallography, fluorescence-based assays and site-directed mutagenesis to determine the structures and functions of these complexes.

Cryo electron microscopy, cryo electron tomography, electron crystallography, membrane protein biochemistry, X-ray crystallography.

Selected Reading
Gatsogiannis C, Merino F, Prumbaum D, Roderer D, Leidreiter F, Meusch D, Raunser S. Membrane insertion of a Tc toxin in near-atomic detail. Nat Struct Mol Biol 2016 (Epub ahead of print)

von der Ecken J, Heissler SM, Pathan-Chhatbar S, Manstein DJ, Raunser S Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution. Nature 2016, 534(7609):724-8.

Friese A, Faesen AC, Huis in 't Veld PJ, Fischböck J, Prumbaum D, Petrovic A, Raunser S, Herzog F, Musacchio A. Molecular requirements for the inter-subunit interaction and kinetochore recruitment of SKAP and Astrin. Nat Commun 2016, 7:11407.

Whitney JC, Quentin D, Sawai S, LeRoux M, Harding BN, Ledvina HE, Tran BQ, Robinson H, Goo YA, Goodlett DR, Raunser S, Mougous JD. An Interbacterial NAD(P)(+) Glycohydrolase Toxin Requires Elongation Factor Tu for Delivery to Target Cells. Cell 2015, 163(3):607-19.

Poepsel S, Sprengel A, Sacca B, Kaschani F, Kaiser M, Gatsogiannis C, Raunser S, Clausen T, Ehrmann M (2015) Determinants of amyloid fibril degradation by the PDZ protease HTRA1. Nat Chem Biol 2015, 11(11):862-9.

Gao M, Berghaus M, von der Ecken J, Raunser S, Winter R. Condensation Agents Determine the Temperature-Pressure Stability of F-Actin Bundles. Angew Chem Int Ed Engl 2015, 54(38):11088-92.

Raunser S, Gatsogiannis C. Deciphering the tubulin code. Cell 2015, 161(5):960-1.

Rosin C, Erlkamp M, Ecken Jv, Raunser S, Winter R. Exploring the stability limits of actin and its suptrastructures, Biophys J 2014, 107(12):2973-83.

Gatsogiannis C, Hofnagel O, Markl J, Raunser S. Structure of Mega-Hemocyanin reveals protein origami in snails, Structure 2015, 23(1):93-103.

von der Ecken J, Müller M, Lehman W, Manstein DJ, Penczek PA, Raunser S. Structure of the F-actin-tropomyosin complex, Nature 2015, 519(7541):114-7.

Meusch D, Gatsogiannis C, Efremov RG, Lang AE, Hofnagel O, Vetter IR, Aktories K, Raunser S. Mechanism of Tc toxin action revealed in molecular detail. Nature 2014, 508(7494), 61-5.

Sadian Y, Gatsogiannis C, Patasi C, Hofnagel O, Goody RS, Farkasovský M, Raunser S. The role of Cdc42 and Gic1 in the regulation of septin filament formation and dissociation. ELife 2013, 2:e01085.

Gatsogiannis C, Lang AE, Meusch D, Pfaumann V, Hofnagel O, Benz R, Aktories K, Raunser S. A syringe-like injection mechanism in Photorhabdus luminescens toxins. Nature 2013, 495(7442), 520-23.

Behrmann E, Müller M, Penczek PA, Mannherz HG, Manstein DJ, Raunser S. Structure of the rigor actin-tropomyosin-myosin complex. Cell 2012, 150(2), 327-339.

Hernandez JM, Stein A, Behrmann E, Riedel D, Cypionka A, Farsi Z, Walla PJ, Raunser S, Jahn R. Membrane fusion intermediates via directional and full assembly of the SNARE complex. Science 2012, 336(6088), 1581-4.

Bröcker C, Kuhlee A, Gatsogiannis C, Balderhaar HJ, Hönscher C, Engelbrecht-Vandré S, Ungermann C, Raunser S. Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex. Proc Natl Acad Sci USA 2012, 109(6), 1991-96.


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