Researcher Portfolio

 
   

Kühlbrandt, Werner

Department of Biophysics, King's College, London WC2B 5RL, United Kingdom, Department of Pure and Applied Biology, Imperial College of Science and Technology, London SW7 2BZ, United Kingdom, Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, European Molecular Biology Laboratory, 6900 Heidelberg, Germany, Institute for Cell Biology, Federal Institute of Technology, CH‐8093 Zürich, Switzerland, Max Planck Institute for Molecular Genetics, Max Planck Society, Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England  

 

Researcher Profile

 
Position: Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society
Position: European Molecular Biology Laboratory, 6900 Heidelberg, Germany
Position: Institute for Cell Biology, Federal Institute of Technology, CH‐8093 Zürich, Switzerland
Position: Department of Pure and Applied Biology, Imperial College of Science and Technology, London SW7 2BZ, United Kingdom
Position: Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England
Position: Max Planck Institute for Molecular Genetics, Max Planck Society
Position: Department of Biophysics, King's College, London WC2B 5RL, United Kingdom
Additional IDs: ORCID: https://orcid.org/0000-0002-2013-4810
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons137764

External references

 
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Publications

 
  (1 - 25 of 247)
 : Introini, B., Hahn, A., & Kühlbrandt, W. (2025). Cryo-EM structure of the NDH-PSI-LHCI supercomplex from Spinacia oleracea. Nature Structural & Molecular Biology. doi:10.1038/s41594-024-01478-1. [PubMan] : Periasamy, A., Ornelas, P., Bausewein, T., Mitchell, N., Zhao, J., Quinn, L. M., Kuehlbrandt, W., & Gulbis, J. M. (2025). Structure of an ex vivoDrosophila TOM complex determined by single-particle cryoEM. IUCrJ, 12(1). doi:10.1107/S2052252524011011. [PubMan] : Dietrich, L., Agip, A.-N.-A., Kunz, C., Schwarz, A., & Kühlbrandt, W. (2024). In situ structure and rotary states of mitochondrial ATP synthase in whole Polytomella cells. Science, 385(6713), 1086-1090. doi:10.1126/science.adp4640. [PubMan] : Schneider, S., Kühlbrandt, W., & Yildiz, Ö. (2024). Complementary structures of the yeast phosphate transporter Pho90 provide insights into its transport mechanism. Structure, 32(7), 979-988.e4. doi:10.1016/j.str.2024.04.005. [PubMan] : Ornelas, P., Bausewein, T., Martin, J., Morgner, N., Nussberger, S., & Kühlbrandt, W. (2023). 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. doi:10.1073/pnas.2301447120. [PubMan] : Klusch, N., Dreimann, M., Senkler, J., Rugen, N., Kühlbrandt, W., & Braun, H.-P. (2023). Cryo-EM structure of the respiratory I + III2 supercomplex from Arabidopsis thaliana at 2 Å resolution. Nature Plants, 9, 142-156. doi:10.1038/s41477-022-01308-6. [PubMan] : Wieferig, J.-P., & Kühlbrandt, W. (2023). Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III2 by cryo-EM. IUCrJ, 10(1), 27-37. doi:10.1107/S2052252522010570. [PubMan] : Laube, E., Meier-Credo, J., Langer, J. D., & Kühlbrandt, W. (2022). Conformational changes in mitochondrial complex I of the thermophilic eukaryote Chaetomium thermophilum. Science Advances, 8(47): eadc9952. doi:10.1126/sciadv.adc9952. [PubMan] : Schiller, J., Laube, E., Wittig, I., Kühlbrandt, W., Vonck, J., & Zickermann, V. (2022). Insights into complex I assembly: Function of NDUFAF1 and a link with cardiolipin remodeling. Science Advances, 8(46): eadd3855. doi:10.1126/sciadv.add3855. [PubMan] : Kühlbrandt, W. (2022). Concluding remarks: Challenges and future developments in biological electron cryo-microscopy. Faraday Discussions, 240, 323-335. doi:10.1039/D2FD90062A. [PubMan] : Lee, Y., Haapanen, O., Altmeyer, A., Kühlbrandt, W., Sharma, V., & Zickermann, V. (2022). Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations. Nature Communications, 13(1): 6091. doi:10.1038/s41467-022-33640-y. [PubMan] : Lee, Y., Wiriyasermkul, P., Kongpracha, P., Moriyama, S., Mills, D. J., Kühlbrandt, W., & Nagamori, S. (2022). Ca2+-mediated higher-order assembly of heterodimers in amino acid transport system b0,+ biogenesis and cystinuria. Nature Communications, 13: 2708. doi:10.1038/s41467-022-30293-9. [PubMan] : Kühlbrandt, W. (2022). Forty years in cryoEM of membrane proteins. Microscopy, 71(Supplement 1), i30-i50. doi:10.1093/jmicro/dfab041. [PubMan] : Ellinghaus, T. L., Marcellino, T., Srinivasan, V., Lill, R., & Kühlbrandt, W. (2021). Conformational changes in the yeast mitochondrial ABC transporter Atm1 during the transport cycle. Science Advances, 7(52): eabk2392. doi:10.1126/sciadv.abk2392. [PubMan] : Parey, K., Lasham, J., Mills, D. J., Djurabekova, A., Haapanen, O., Yoga, E. G., Xie, H., Kühlbrandt, W., Sharma, V., Vonck, J., & Zickermann, V. (2021). High-resolution structure and dynamics of mitochondrial complex I-Insights into the proton pumping mechanism. Science Advances, 7(46): eabj3221. doi:10.1126/sciadv.abj3221. [PubMan] : Heit, S., Geurts, M. M. G., Murphy, B. J., Corey, R. A., Mills, D. J., Kühlbrandt, W., & Bublitz, M. (2021). Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state. Science Advances, 7(46): eabj5255. doi:10.1126/sciadv.abj5255. [PubMan] : Klusch, N., Senkler, J., Yildiz, Ö., Kühlbrandt, W., & Braun, H.-P. (2021). A ferredoxin bridge connects the two arms of plant mitochondrial complex I. The Plant Cell, 33(6), 2072-2091. doi:10.1093/plcell/koab092. [PubMan] : Floris, D., & Kühlbrandt, W. (2021). Molecular landscape of etioplast inner membranes in higher plants. Nature Plants, 7(4), 514-523. doi:10.1038/s41477-021-00896-z. [PubMan] : D'Imprima, E., & Kühlbrandt, W. (2021). Current limitations to high-resolution structure determination by single-particle cryoEM. Quarterly Reviews of Biophysics, 54: e4. doi:10.1017/S0033583521000020. [PubMan] : Wieferig, J.-P., Mills, D. J., & Kühlbrandt, W. (2021). Devitrification reduces beam-induced movement in cryo-EM. IUCrJ, 8(Pt 2), 186-194. doi:10.1107/S2052252520016243. [PubMan] : Vögele, M., Bhaskara, R., Mulvihill, E., van Pee, K., Yildiz, Ö., Kühlbrandt, W., Müller, D. J., & Hummer, G. (2020). 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), 5109-5110. doi:10.1073/pnas.1922488117. [PubMan] : Joppe, M., D'Imprima, E., Salustros, N., Paithankar, K. S., Vonck, J., Grininger, M., & Kühlbrandt, W. (2020). 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), 220-227. doi:10.1107/S2052252519017366. [PubMan] : Warnau, J., Wöhlert, D., Okazaki, K.-I., Yildiz, Ö., Gamiz-Hernandez, A. P., Kaila, V. R. I., Kühlbrandt, W., & Hummer, G. (2020). Ion Binding and Selectivity of the Na+/H+ Antiporter MjNhaP1 from Experiment and Simulation. The Journal of Physical Chemistry B, 124(2), 336-344. doi:10.1021/acs.jpcb.9b08552. [PubMan] : Parey, K., Haapanen, O., Sharma, V., Köfeler, H., Züllig, T., Prinz, S., Siegmund, K., Wittig, I., Mills, D., Vonck, J., Kühlbrandt, W., & Zickermann, V. (2019). High-resolution cryo-EM structures of respiratory complex I: Mechanism, assembly, and disease. Science Advances, 5(12), eaax9484. doi:10.1126/sciadv.aax9484. [PubMan] : Pfeil-Gardiner, O., Mills, D. J., Vonck, J., & Kühlbrandt, W. (2019). A comparative study of single-particle cryo-EM with liquid-nitrogen and liquid-helium cooling. IUCrJ, 6, 1099-1105. doi:10.1107/S2052252519011503. [PubMan]