Periasamy, A.; Ornelas, P.; Bausewein, T.; Mitchell, N.; Zhao, J.; Quinn, L. M.; Kuehlbrandt, W.; Gulbis, J. M.: Structure of an ex vivoDrosophila TOM complex determined by single-particle cryoEM. IUCrJ 12 (1) (2025)
Dietrich, L.; Agip, A.-N. A.; Kunz, C.; Schwarz, A.; Kühlbrandt, W.: In situ structure and rotary states of mitochondrial ATP synthase in whole Polytomella cells. Science 385 (6713), pp. 1086 - 1090 (2024)
Schneider, S.; Kühlbrandt, W.; Yildiz, Ö.: Complementary structures of the yeast phosphate transporter Pho90 provide insights into its transport mechanism. Structure 32 (7), pp. 979 - 988.e4 (2024)
Ornelas, P.; Bausewein, T.; Martin, J.; Morgner, N.; Nussberger, S.; Kühlbrandt, W.: Two conformations of the Tom20 preprotein receptor in the TOM holo complex. Proceedings of the National Academy of Sciences of the United States of America 120 (34), e2301447120 (2023)
Klusch, N.; Dreimann, M.; Senkler, J.; Rugen, N.; Kühlbrandt, W.; Braun, H.-P.: Cryo-EM structure of the respiratory I + III2 supercomplex from Arabidopsis thaliana at 2 Å resolution. Nature Plants 9, pp. 142 - 156 (2023)
Wieferig, J.-P.; Kühlbrandt, W.: Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III2 by cryo-EM. IUCrJ 10 (1), pp. 27 - 37 (2023)
Schiller, J.; Laube, E.; Wittig, I.; Kühlbrandt, W.; Vonck, J.; Zickermann, V.: Insights into complex I assembly: Function of NDUFAF1 and a link with cardiolipin remodeling. Science Advances 8 (46), eadd3855 (2022)
Kühlbrandt, W.: Concluding remarks: Challenges and future developments in biological electron cryo-microscopy. Faraday Discussions 240, pp. 323 - 335 (2022)
Ellinghaus, T. L.; Marcellino, T.; Srinivasan, V.; Lill, R.; Kühlbrandt, W.: Conformational changes in the yeast mitochondrial ABC transporter Atm1 during the transport cycle. Science Advances 7 (52), eabk2392 (2021)
Heit, S.; Geurts, M. M. G.; Murphy, B. J.; Corey, R. A.; Mills, D. J.; Kühlbrandt, W.; Bublitz, M.: Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state. Science Advances 7 (46), eabj5255 (2021)
Klusch, N.; Senkler, J.; Yildiz, Ö.; Kühlbrandt, W.; Braun, H.-P.: A ferredoxin bridge connects the two arms of plant mitochondrial complex I. The Plant Cell 33 (6), pp. 2072 - 2091 (2021)
D'Imprima, E.; Kühlbrandt, W.: Current limitations to high-resolution structure determination by single-particle cryoEM. Quarterly Reviews of Biophysics 54, e4 (2021)
Vögele, M.; Bhaskara, R.; Mulvihill, E.; van Pee, K.; Yildiz, Ö.; Kühlbrandt, W.; Müller, D. J.; Hummer, G.: Reply to Desikan et al.: Micelle formation among various mechanisms of toxin pore formation. Proceedings of the National Academy of Sciences of the United States of America 117 (10), pp. 5109 - 5110 (2020)
Joppe, M.; D'Imprima, E.; Salustros, N.; Paithankar, K. S.; Vonck, J.; Grininger, M.; Kühlbrandt, W.: The resolution revolution in cryoEM requires high-quality sample preparation: a rapid pipeline to a high-resolution map of yeast fatty acid synthase. IUCrJ 7 (Pt 2), pp. 220 - 227 (2020)
Warnau, J.; Wöhlert, D.; Okazaki, K.-I.; Yildiz, Ö.; Gamiz-Hernandez, A. P.; Kaila, V. R. I.; Kühlbrandt, W.; Hummer, G.: Ion Binding and Selectivity of the Na+/H+ Antiporter MjNhaP1 from Experiment and Simulation. The Journal of Physical Chemistry B 124 (2), pp. 336 - 344 (2020)
Vögele, M.; Bhaskara, R.; Mulvihill, E.; van Pee, K.; Yildiz, Ö.; Kühlbrandt, W.; Müller, D. J.; Hummer, G.: Membrane perforation by the pore-forming toxin pneumolysin. Proceedings of the National Academy of Sciences of the United States of America 116 (27), pp. 13352 - 13357 (2019)
Blum, T.; Hahn, A.; Meier, T.; Davies, K. M.; Kühlbrandt, W.: Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows. Proceedings of the National Academy of Sciences of the United States of America 116 (10), pp. 4250 - 4255 (2019)
Sousa, J. S.; Calisto, F.; Langer, J. D.; Mills, D. J.; Refojo, P. N.; Teixeira, M.; Kühlbrandt, W.; Vonck, J.; Pereira, M. M.: Structural basis for energy transduction by respiratory alternative complex III. Nature Communications 9, 1728 (2018)
Davies, K. M.; Blum, T. B.; Kühlbrandt, W.: Conserved in situ arrangement of complex I and III2 in mitochondrial respiratory chain supercomplexes of mammals, yeast, and plants. Proceedings of the National Academy of Sciences of the United States of America 115 (12), pp. 3024 - 3029 (2018)
Davies, K. M.; Kühlbrandt, W.: Structure of the catalytic F1 head of the F1-Fo ATP synthase from Trypanosoma brucei. Proceedings of the National Academy of Sciences of the United States of America 115 (13), pp. E2906 - E2907 (2018)
Mühleip, A. W.; Dewar, C. E.; Schnaufer, A.; Kühlbrandt, W.; Davies, K. M.: In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits. Proceedings of the National Academy of Sciences of the United States of America 114 (5), pp. 992 - 997 (2017)
Retel, J. S.; Nieuwkoop, A. J.; Hiller, M.; Higman, V. A.; Barbet-Massin, E.; Stanek, J.; Andreas, L. B.; Franks, W. T.; van Rossum, B.-J.; Vinothkumar, K. R.et al.; Handel, L.; de Palma, G. G.; Bardiaux, B.; Pintacuda, G.; Emsley, L.; Kühlbrandt, W.; Oschkinat, H.: Structure of outer membrane protein G in lipid bilayers. Nature Communications 8, 2073, p. 1 (2017)
Wilkes, M.; Madej, G. M.; Kreuter, L.; Rhinow, D.; Heinz, V.; De Sanctis, S.; Ruppel, S.; Richter, R. M.; Joos, F.; Grieben, M.et al.; Pike, A. C. W.; Huiskonen, J. T.; Carpenter, E. P.; Kühlbrandt, W.; Witzgall, R.: Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2. Nature Structural and Molecular Biology 24 (2), pp. 123 - 130 (2017)
Hahn, A.; Parey, K.; Bublitz, M.; Mills, D. J.; Zickermann, V.; Vonck, J.; Kühlbrandt, W.; Meier, T.: Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology. Molecular Cell 63, pp. 1 - 12 (2016)
Mühleip, A. W.; Joos, F.; Wigge, C.; Frangakis, A. S.; Kühlbrandt, W.; Davies, K. M.: Helical arrays of U-shaped ATP synthase dimers form tubular cristae in ciliate mitochondria. Proceedings of the National Academy of Sciences of the United States of America 113 (30), pp. 8442 - 8447 (2016)
Subramaniam, S.; Kühlbrandt, W.; Henderson, R.: CryoEM at IUCrJ: a new era. International Union of Crystallography Journal (IUCrJ) 3 (1), pp. 3 - 7 (2016)
Bohnert, M.; Zerbes, R. M.; Davies, K. M.; Mühleip, A. W.; Rampelt, H.; Horvath, S. E.; Boenke, T.; Kram, A.; Perschil, I.; Veenhuis, M.et al.; Kühlbrandt, W.; van der Klei, I. J.; Pfanner, N.; van der Laan, M.: Central Role of Mic10 in the Mitochondrial Contact Site and Cristae Organizing System. Cell Metabolism 21 (5), pp. 747 - 755 (2015)
Kukat, C.; Davies, K. M.; Wurm, C. A.; Spåhr, H.; Bonekamp, N. A.; Kühl, I.; Joos, F.; Polosa, P. L.; Park, C. B.; Posse, V.et al.; Falkenberg, M.; Jakobs, S.; Kühlbrandt, W.; Larsson, N.-G.: Cross-strand binding of TFAM to a single mtDNA molecule forms the mitochondrial nucleoid. Proceedings of the National Academy of Sciences of the United States of America 112 (36), pp. 11288 - 11293 (2015)
Vrandecic, K.; Rätsep, M.; Wilk, L.; Rusevich, L.; Golub, M.; Reppert, M.; Irrgang, K.-D.; Kühlbrandt, W.; Pieper, J.: Protein Dynamics Tunes Excited State Positions in Light-Harvesting Complex II. The Journal of Physical Chemistry B 119 (10), pp. 3920 - 3930 (2015)
Gold, V. A. M.; Ieva, R.; Walter, A.; Pfanner, N.; van der Laan, M.; Kühlbrandt, W.: Visualizing active membrane protein complexes by electron cryotomography. Nature Communications 5, 4129 (2014)
Allegretti, M.; Mills, D. J.; McMullen, G.; Kühlbrandt, W.; Vonck, J.: Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector. eLife 3, e01963 (2014)
Daum, B.; Quax, T. E. F.; Sachse, M.; Mills, D. J.; Reimann, J.; Yildiz, Ö.; Häder, S.; Saveanu, C.; Forterre, P.; Albers, S.-V.et al.; Kühlbrandt, W.; Prangishvili, D.: Self-assembly of the general membrane-remodeling protein PVAP into sevenfold virus-associated pyramids. Proceedings of the National Academy of Sciences of the United States of America 111 (10), pp. 3829 - 3834 (2014)
Köster, S.; van Pee, K.; Hudel, M.; Leustik, M.; Rhinow, D.; Kühlbrandt, W.; Chakraborty, T.: Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation. Nature Communications 5, 3690 (2014)
Quemin, E. R. J.; Lucas, S.; Daum, B.; Quax, T. E. F.; Kühlbrandt, W.; Forterre, P.; Albers, S.-V.; Prangishvili, D.; Krupovic, M.: First insights into the entry process of hyperthermophilic archaeal viruses. Journal of Virology 87 (24), pp. 13379 - 13385 (2013)
Kalayil, S.; Schulze, S.; Kühlbrandt, W.: Arginine oscillation explains Na+ independence in the substrate/product antiporter CaiT. Proceedings of the National Academy of Sciences of the United States of America 110 (43), pp. 17296 - 17301 (2013)
Daum, B.; Walter, A.; Horst, A.; Osiewacz, H. D.; Kühlbrandt, W.: Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria. Proceedings of the National Academy of Sciences of the United States of America 110 (38), pp. 15301 - 15306 (2013)
Wilk, L.; Grunwald, M.; Liao, P.-N.; Walla, P. J.; Kühlbrandt, W.: Direct interaction of the major light-harvesting complex II and PsbS in nonphotochemical quenching. Proceedings of the National Academy of Sciences of the United States of America 110 (14), pp. 5452 - 5456 (2013)
Davies, K. M.; Anselmi, C.; Wittig, I.; Faraldo-Gómez, J. D.; Kühlbrandt, W.: Structure of the yeast F1F0-ATP synthase dimer and its role in shaping the mitochondrial cristae. Proceedings of the National Academy of Sciences of the United States of America 109 (34), pp. 13602 - 13607 (2012)
Köster, S.; Pavkov-Keller, T.; Kühlbrandt, W.; Yildiz, Ö.: Structure of Human Na+/H+ Exchanger NHE1 Regulatory Region in Complex with Calmodulin and Ca2+. The Journal of Biological Chemistry 286 (47), pp. 40954 - 40961 (2011)
Müller, M.; Bamann, C.; Bamberg, E.; Kühlbrandt, W.: Projection Structure of Channelrhodopsin-2 at 6 Å Resolution by Electron Crystallography. Journal of Molecular Biology 414 (1), pp. 86 - 95 (2011)
Wilk, L.; Strauss, M.; Rudolf, M.; Nicolaisen, K.; Flores, E.; Kühlbrandt, W.; Schleiff, E.: Outer membrane continuity and septosome formation between vegetative cells in the filaments of Anabaena sp. PCC 7120. Cellular Microbiology 13 (11), pp. 1744 - 1754 (2011)
Davies, K. M.; Strauss, M.; Daum, B.; Kief, J. H.; Osiewacz, H. D.; Rycovska, A.; Zickermann, V.; Kühlbrandt, W.: Macromolecular organization of ATP synthase and complex I in whole mitochondria. Proceedings of the National Academy of Sciences of the United States of America 108 (34), pp. 14121 - 14126 (2011)
Researchers at the Max Planck Institute of Biophysics and the University of Cologne developed a new optical tool to study ferroptosis, a form of iron-driven cell death. Better understanding of how it spreads could open doors to new therapies.
On February 5, 2024, we participated in the “Frankfurt Stands Up for Democracy” demonstration, standing alongside nearly 20,000 participants representing over 100 institutions, organizations, and companies across the Frankfurt region.
The Max Planck Institute of Biophysics is part of the new science network Frankfurt Alliance together with 15 other research institutions in the Rhine-Main metropolitan area
The fellow program promotes cooperation between Max Planck Institutes and outstanding professors at universities. From March 2024, Müller-McNicoll will lead a small research group at the MPI in Frankfurt for five years to investigate RNA, the carrier of genetic information in the cell, and its regulation.