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)
Cunha, E. S.; Chen, X.; Sanz-Gaitero, M.; Mills, D. J.; Luecke, H.: Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution. Nature Communications 12 (1), 230 (2021)
Ebenhoch, R.; Prinz, S.; Kaltwasser, S.; Mills, D. J.; Meinecke, R.; Rübbelke, M.; Reinert, D.; Bauer, M.; Weixler, L.; Zeeb, M.et al.; Vonck, J.; Nar, H.: A hybrid approach reveals the allosteric regulation of GTP cyclohydrolase I. Proceedings of the National Academy of Sciences of the United States of America 117 (50), pp. 31838 - 31849 (2020)
Wu, D.; Grund, T. N.; Welsch, S.; Mills, D.; Michel, M.; Safarian, S.; Michel, H.: Structural basis for amino acid exchange by a human heteromeric amino acid transporter. Proceedings of the National Academy of Sciences of the United States of America 117 (35), 202008111, pp. 21281 - 21287 (2020)
Tascón, I.; Sousa, J. S.; Corey, R. A.; Mills, D. J.; Griwatz, D.; Aumüller, N.; Mikusevic, V.; Stansfeld, P. J.; Vonck, J.; Hänelt, I.: Structural basis of proton-coupled potassium transport in the KUP family. Nature Communications 11, 626 (2020)
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)
Diskowski, M.; Mehdipour, A. R.; Wunnicke, D.; Mills, D. J.; Mikusevic, V.; Bärland, N.; Hoffmann, J.; Morgner, N.; Steinhoff, H.-J.; Hummer, G.: Helical jackknives control the gates of the double-pore K+ uptake system KtrABs. eLife, pp. 1 - 21 (2017)
Kohler, R.; Mooney, R. A.; Mills, D. J.; Landick, R.; Cramer, P.: Architecture of a transcribing-translating expressome. Science 356, pp. 194 - 197 (2017)
López-Alonso, J. P.; Kaminishi, T.; Kikuchi, T.; Hirata, Y.; Iturrioz, I.; Dhimole, N.; Schedlbauer, A.; Hase, Y.; Goto, S.; Kurita, D.et al.; Muto, A.; Zhou, S.; Naoe, C.; Mills, D. J.; Gil-Carton, D.; Takemoto, C.; Himeno, H.; Fucini, P.; Connell, S. R.: RsgA couples the maturation state of the 30S ribosomal decoding center to activation of its GTPase pocket. Nucleic Acids Research 45 (11), pp. 6945 - 6959 (2017)
Vonck, J.; Parcej, D. N.; Mills, D. J.: Structure of Alcohol Oxidase from Pichia pastoris by Cryo-Electron Microscopy. PLOS ONE 11 (7), e0159476 (2016)
Chaudhury, P.; Neiner, T.; D'Imprima, E.; Banerjee, A.; Reindl, S.; Ghosh, A.; Arvai, A. S.; Mills, D. J.; van der Does, C.; Tainer, J. A.et al.; Vonck, J.; Albers, S.: The nucleotide-dependent interaction of FlaH and FlaI isessential for assembly and function of the archaellum motor. Molecular Microbiology 99 (4), pp. 674 - 685 (2016)
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)
Fischer, M.; Rhinow, D.; Zhu, Z.; Mills, D. J.; Zhao, Z. K.; Vonck, J.; Grininger, M.: Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS. Protein Science 24 (6), pp. 987 - 995 (2015)
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)
Mills, D. J.; Vitt, S.; Strauss, M.; Shima, S.; Vonck, J.: De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy. eLife 2, e00218 (2013)
Ciccarelli, L.; Connell, S. R.; Enderle, M.; Mills, D. J.; Vonck, J.; Grininger, M.: Structure and Conformational Variability of the Mycobacterium tuberculosis Fatty Acid Synthase Multienzyme Complex. Structure 21 (7), pp. 1251 - 1257 (2013)
Banerjee, A.; Ghosh, A.; Mills, D. J.; Kahnt, J.; Vonck, J.; Albers, S.-V.: FlaX, A Unique Component of the Crenarchaeal Archaellum, Forms Oligomeric Ring-shaped Structures and Interacts with the Motor ATPase FlaI. The Journal of Biological Chemistry 287 (52), pp. 43322 - 43330 (2012)
Althoff, T.; Mills, D. J.; Popot, J.-L.; Kühlbrandt, W.: Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. EMBO Journal 30, pp. 4652 - 4664 (2011)
Gipson, P.; Mills, D. J.; Wouts, R.; Grininger, M.; Vonck, J.; Kühlbrandt, W.: Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy. Proceedings of the National Academy of Sciences of the United States of America 107 (20), pp. 9164 - 9169 (2010)
Kamal, M. M.; Mills, D.; Grzybeck, M.; Howard, J.: Measurement of the membrane curvature preference of phospholipids reveals only weak coupling between lipid shape and leaflet curvature. Proceedings of the National Academy of Sciences of the United States of America 106 (52), pp. 22245 - 22250 (2009)
Schmidt-Krey, I.; Kanaoka, Y.; Mills, D. J.; Lam, B. K.; Irikura, D.; Haase, W.; Austen, K. F.; Kühlbrandt, W.: Human Leukotriene C4 Synthase at 4.5 Å Resolution in Projection. Structure 12, pp. 2009 - 2014 (2004)
Behlau, M.; Mills, D. J.; Quader, H.; Kühlbrandt, W.; Vonck, J.: Projection structure of the monomeric porin OmpG at 6 å resolution. Journal of Molecular Biology (London) 305 (1), pp. 71 - 77 (2001)
Mills, D. J.; Vonck, J.: Choice and Maintenance of Equipment for Electron Crystallography. In: Electron Crystallography of Soluble and Membrane Proteins: Methods and Protocols, Vol. 995, pp. 331 - 351 (Eds. Schmidt-Krey, I.; Cheng, Y.). Springer Science+Business Media New York 2013, Humana Totowa, NJ (2013)
The cryo EM structure of respiratory complex I from Yarrowia lipolytica (Biochim. Biophys. Acta (BBA) - Bioenergetics, 1859). Budapest, Hungary (2018), 01 p.
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.