Max Planck Institute of Biophysics

Max Planck Institute of Biophysics

The Max Planck Institute of Biophysics focuses on investigating the structure and function of proteins that are embedded in cellular membranes. Membrane proteins functioning as channels, transporters, or molecular sensors mediate the exchange of matter and information of cells with their environment. Scientists at the Institute use electron microscopes and X-rays to determine the spatial structure of these proteins. In addition, protein function is characterized by electrophysiology, a technique which measures the electric currents and voltages generated when electrically-charged atoms (ions) flow through membrane proteins. As an ideal complement to the experimental characterizations, these molecular processes are also studied theoretically to develop quantitative descriptions and to gain a detailed understanding of the underlying mechanisms.


Max-von-Laue-Straße 3
60438 Frankfurt am Main
Phone: +49 69 6303-0
Fax: +49 69 6303-4502

PhD opportunities

This institute has no International Max Planck Research School (IMPRS).

There is always the possibility to do a PhD. Please contact the directors or research group leaders at the Institute.

Structure of channelrhodopsin determined
Researchers discover structure and mechanism of action of molecular light switch, paving the way for new applications more
Information filter for immune defence
Researchers are deciphering the structure of the MHC-I peptide-loading complex. more
By using innovative labeling methods, Max Planck researchers develop a technique to measure newly synthesized proteins in the active mouse brain more
Optogenetics: Sodium pump could act as light switch
The structure of the light-driven ion pump KR2 may provide a blueprint for new optogenetic tools more
Optogenetics – Combination switch turns neurons on and off
Max Planck scientists control neurons using two linked light channels more
Max Planck Innovation gets caesar spin-off KonTEM under way
Spin-off company develops phase contrast for electron microscopy more
Gene switch for odorant receptors

Gene switch for odorant receptors

News November 10, 2011
Tiny regulatory elements in the genome regulate the probability that olfactory sensory neurons choose a particular odorant receptor gene for expression more
Max Planck Society partners with Sanofi to develop innovative solutions for restoring vision
New collaboration reinforces Sanofi’s translational discovery platform for retinal diseases more
Ultra light-sensitive and fast light switches for nerve cells
The use of a highly light-sensitive membrane protein enables precise control of nerve cell activity with weak light stimuli. more
Light switches for nerve cells

Light switches for nerve cells

News April 06, 2010
Max Planck scientists revolutionize neurobiology and win coveted science prize more

Custom-Tailored Molecules

4/2014 Biology & Medicine
Chlamydomonas reinhardtii, a single-celled green alga, can’t see much at all with its eye composed solely of photosensitive rhodopsin molecules. Yet there is more to algal rhodopsin than one would expect. In recent years, it has triggered a revolution in neurobiology. Ernst Bamberg from the Max Planck Institute of Biophysics in Frankfurt helped make it famous. He is now researching these molecules and developing new variants for basic research and medical applications.
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Structure of dimeric ATP synthase from the inner membrane of yeast mitochondria

2017 Hahn, Alexander; Parey, Kristian; Bublitz, Maike; Mills, Deryck J.; Zickermann, Volker; Vonck, Janet; Kühlbrandt, Werner; Meier, Thomas
Cell Biology Structural Biology
We determined the structure of a complete, dimeric F1Fo-ATP synthase from mitochondria of the yeast Yarrowia lipolytica by a combination of cryo-electron microscopy (cryo-EM) and X-ray crystallography. The structure resolves 58 of the 60 subunits in the dimer. Horizontal helices of subunit a in Fo wrap around the c-ring rotor, and a total of six vertical helices assigned to subunits a, b, f, i, and 8 span the membrane. Our data explain the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology. more

How nature reduces molecular oxygen to water conserving energy at the same time

2016 Michel, Hartmut; Ermler, Ulrich; Safarian, Schara
Structural Biology
Molecular oxygen appeared in the atmosphere about three billion years ago. Nature developed two membrane integrated enzymatic systems which reduce oxygen to water and use the energy of this reaction to produce biologically important energy carriers. These enzymes are the haem-copper terminal oxidases, e.g. cytochrome c oxidase, and the bd oxidases. The atomic structures of representative members of both enzyme families were determined. These evolutionary unrelated enzymes apparently use the same mechanisms to conserve energy and to prevent the formation of toxic reactive oxygen species. more

Molecular Simulations: from biomolecular structures to function

2015 Hummer, Gerhard
Cell Biology Computer Science Evolutionary Biology Genetics Structural Biology
Molecular simulations allow us to study the functional mechanisms of biomolecules. Thanks to their enormously detailed description, by resolving the motion of every atom, such simulations help to interpret complex experiments. Simulations also allow us to venture into areas which are difficult to access by experiments, such as the detailed characterization of enzymatic reaction mechanisms. Moreover, by “watching proteins at work”, new and fundamental processes can be discovered by using molecular simulations. more

Current Research in Structural Biology

2014 Werner Kühlbrandt
Cell Biology Structural Biology
The Department elucidates the structure and function of membrane proteins as well as macromolecular protein complexes by using electron microscopy, x-ray crystallography, biochemical and biophysical methods. It consists of a group lead by director Werner Kühlbrandt and project groups operated by Janet Vonck and Özkan Yildiz. Thomas Meier and Daniel Rhinow run two independent research groups. Christine Ziegler, now appointed as professor at the University of Regensburg, is still associated with the Department. Here, we present current data and results from all over the Department’s research. more

GcpE and LytB: Enzymes of isoprenoid biosynthesis as targets for drugs against malaria and tuberculosis

2013 Rekittke, Ingo; Jomaa, Hassan; Ermler, Ulrich
Cell Biology Physiology Structural Biology
Isoprenoids are involved in vital processes of all organisms. Their biosynthesis proceeds via two C5-building blocks, which are produced dependent on the organism either by the mevalonate- or the desoxyxylose (DOXP) pathway. The DOXP pathway is used by various human pathogens but not by man and therefore provides an attractive target for anti-infectious agents, e.g., against malaria and tuberculosis. more

Optogenetics: The molecular basis and applications

2012 Bamberg, Ernst
The new field of optogenetics describes mainly the use of the light-gated ion channel, Channelrhodopsin 2 (ChR2) and of the light-driven Cl-pump Halorhodopsin (NphR) for stimulation and silencing of neurons simply by light in cultured cells as well as in brains of living animals. In order to increase the possibilities of application we have focused our research to develop new and improved tools. more

Structure and Function of Membrane Proteins

2011 Kühlbrandt, Werner
Structural Biology
The research of the Department of Structural Biology focuses on understanding the structural basis of membrane transport and biological energy conversion at the highest possible level of detail. The main methods are crystallography of membrane protein crystals (2D and 3D), single-particle cryo-EM and electron cryo-tomography (cryo-ET) of biological membranes. With few exceptions, all membrane proteins for crystallography, as well as membranes or organelles for tomography are produced within the group. more
Remote control of neural cells by light by means of the light-gated cation channel Channelrhodopsin2 (ChR2) and of the light-driven Cl- pump Halorhodopsin (NphR) fulfils a long lasting desire of neurobiologists. With this method neurons in culture as well as in the brain of living animals can be activated or inactivated at different wavelengths of the exciting light in a non invasive, electrode free manner with high temporal and even more important with an up to now unknown spatial resolution. This new technique has set the basis for the fast developing field of optogenetics. more

Molecular Neurogenetics of the Mouse Olfactory System

2009 Spors, Hartwig; Mombaerts, Peter
In the mouse, the sense of smell (olfaction) is mediated by more than 1200 odorant receptors (ORs), the largest gene family in the genome. These ORs are G-protein coupled receptors. Every olfactory sensory neuron (OSN) in the main olfactory epithelium is thought to express just one OR gene, from one allele. Axons of OSNs that express the same OR coalesce into the same structures in the olfactory bulb, termed glomeruli, where they form synapses with second-order neurons in the olfactory pathway. more
1. Variants of the mitochondrial cytochrome bc1 complex created by site-directed mutagenesis produce deleterious oxygen radicals, which are implied in aging processes and pathophysiological conditions. 2. The regulation of the cellular ion composition by sodium-proton-antiporters is essential. The first atomic structure of such a transporter was determined and a mechanistic model for regulation and transport developed. more
The atomic structures of a bacterial succinate:quinone oxidoreductase and of mechanistically interesting variants have been determined by X-ray crystallography. Together with complementary functional studies, these results have yielded unequivocal evidence for a novel type of essential transmembrane proton transfer driving transmembrane electron transfer in this protein complex. more

Mechanisms of membrane transport visualized by electron microscopy and x-ray crystallography

2007 Kühlbrandt, Werner; Appel, Matthias; Barton, Bastian; Kalthoff, Christoph; Raunser, Stefan; Schröder, Rasmus; Vinothkumar, Kutti Ragunath; Yildiz, Özkan
Structural Biology
In recent research the Department of Structural Biology at the Max Planck Institute of Biophysics addressed membrane transport proteins from thermophilic archaea, which are more robust than their eukaryotic counterparts yet often quite similar to them, and thus serve as good models for medically relevant systems. They determined the structure of a signaling protein that regulates nitrogen uptake in archaea and bacteria in three different states, which helped them to elucidate the regulatory mechanism. Furthermore they investigated pH- and ion-induced conformational changes that accompany activation and ion transport in sodium-proton exchange proteins, and in the outer membrane porin OmpG from E. coli. more
Phototaxis and photophobic responses of the green alga Chlamydomonas reinhardtii are mediated by microbial rhodopsins with the chromophore retinal. Sequence comparison with other microbial rhodopsins from archaea as the light-driven proton pump bacteriorhodopsin and the light-driven chloride pump halorhodopsin showed an overall homology of 15 to 20 % of those two algae chromoproteins. It is equally important that the N-terminal half approximately 300 of 712 and 737 amino acids, respectively, comprises seven hypothetical transmembrane helices as it is typical for rhodopsin-like proteins. Morover, several of the amino acids are conserved, which define the retinal binding site as well as the H+ -transporting pathway in bacteriorhodopsin. Recently, we demonstrated that two of these retinal-binding proteins from the eyespot of the alga, which we named channelrhodopsin-1 and -2 (ChR1 and ChR2), showed channel activity, directly activated by light when expressed in oocytes from Xenopus laevis or HEK 293 cells. ChR1 is selective for protons, whereas ChR2 is also conductive for monovalent and divalent cations. For both proteins the N-terminal hydrophobic half is sufficient to enable light-gated channel activity, demonstrating that the seven transmembrane helix motif represents a new class of ion channels. more

The One-Carbon Carrier Tetrahydromethanopterin in Enzymes

2005 Ermler, Ulrich; Acharya, Pryamvada
Structural Biology
The one-carbon (C1) carrier tetrahydromethanopterin (H4MPT), that non-covalently binds as cofactor to proteins, became more and more important in the last years, as it was discovered in several phylogenetically distinct microorganisms where it plays a pronounced role in the C1 metabolism. Interestingly, its structure is highly similar to that of tetrahydrofolate (H4F), the most universal C1 carrier in biochemistry, but most likely H4MPT and H4F were separately developed within a convergent evolutionary process. The mode how H4MPT binds to enzymes was recently established on a structural level for two systems that will be introduced. more

Structure and molecular mechanisms of membrane transport proteins

2004 Collinson, Ian; Kühlbrandt, Werner; Model, Kirstin; Parcej, David; Standfuss, Jörg; Terwisscha van Scheltinga, Anke; Ziegler, Christine
Structural Biology
The Department of Structural Biology at the Max Planck Institute of Biophysics focuses on the structure and molecular mechanisms of membrane transport proteins. The structures of membrane proteins purified from natural sources or expressed in suitable host organisms are determined by electron microscopy or x-ray crystallography. The 2.5Å x-ray structure of the plant light-harvesting complex LHC-II reveals the mechanism of photoprotection and a likely pathway for dissipating excess solar energy. A three-dimensional map of a neuronal ion channel, determined by single-particle electron microscopy, shows the position of the alpha and beta subunits in the functional assembly. The 8Å map of the bacterial protein translocase SecYEG in the membrane shows how the structure adapts to the early steps of protein translocation. Structural studies of the protein translocase from outer and inner membranes of mitochondria reveal a twin pore. Two-dimensional crystals of various secondary transporters show different arrangements of membrane-spanning helices, indicative of different transport mechanisms. more
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