Researcher Portfolio
Mills, Deryck
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society
Researcher Profile
Position: Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society
Additional IDs: ORCID:
https://orcid.org/0000-0003-0904-1119
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons137802
Publications
(1 - 25 of 49)
: 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] : 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] : 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] : Cunha, E. S., Chen, X., Sanz-Gaitero, M., Mills, D. J., & Luecke, H. (2021). Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution. Nature Communications, 12(1): 230. doi:10.1038/s41467-020-20485-6. [PubMan] : Mills, D. J. (2021). Setting up and operating a cryo-EM laboratory. Quarterly Reviews of Biophysics, 54: e2. doi:10.1017/S003358352000013X. [PubMan] : Ebenhoch, R., Prinz, S., Kaltwasser, S., Mills, D. J., Meinecke, R., Rübbelke, M., Reinert, D., Bauer, M., Weixler, L., Zeeb, M., Vonck, J., & Nar, H. (2020). 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), 31838-31849. doi:10.1073/pnas.2013473117. [PubMan] : Wu, D., Grund, T. N., Welsch, S., Mills, D., Michel, M., Safarian, S., & Michel, H. (2020). 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. doi:10.1073/pnas.2008111117. [PubMan] : Tascón, I., Sousa, J. S., Corey, R. A., Mills, D. J., Griwatz, D., Aumüller, N., Mikusevic, V., Stansfeld, P. J., Vonck, J., & Hänelt, I. (2020). Structural basis of proton-coupled potassium transport in the KUP family. Nature Communications, 11: 626. doi:10.1038/s41467-020-14441-7. [PubMan] : Brünle, S., Eisinger, M. L., Poppe, J., Mills, D. J., Langer, J. D., Vonck, J., & Ermler, U. (2019). Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism. Proceedings of the National Academy of Sciences of the United States of America, 52(116), 26497-26504. doi:10.1073/pnas.1913031116. [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] : Safarian, S., Hahn, A., Mills, D., Radloff, M., Eisinger, M. L., Nikolaev, A., Meier-Credo, J., Melin, F., Miyoshi, H., Gennis, R., Sakamoto, J., Langer, J. D., Hellwig, P., Kühlbrandt, W., & Michel, H. (2019). Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. Science, 366(6461), 100-104. doi:10.1126/science.aay0967. [PubMan] : Murphy, B. J., Klusch, N., Langer, J. D., Mills, D., Yildiz, Ö., & Kühlbrandt, W. (2019). Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling. Science, 364(6446): eaaw9128, pp. 1155. doi:10.1126/science.aaw9128. [PubMan] : Parey, K., Brandt, U., Xie, H., Mills, D. J., Siegmund, K., Vonck, J., Kühlbrandt, W., & Zickermann, V. (2018). Cryo-EM structure of respiratory complex I at work. eLife, 7: e39213. doi:10.7554/eLife.39213. [PubMan] : Sousa, J. S., Calisto, F., Langer, J. D., Mills, D. J., Refojo, P. N., Teixeira, M., Kühlbrandt, W., Vonck, J., & Pereira, M. M. (2018). Structural basis for energy transduction by respiratory alternative complex III. Nature Communications, 9: 1728. doi:10.1038/s41467-018-04141-8. [PubMan] : Vonck, J., Sousa, J. S., Calisto, F., Mills, D., Langer, J. D., Refojo, P. N., Teixeira, M., Kühlbrandt, W., & Pereira, M. M. (2018). Cryo-EM structure of the alternative complex III from Rhodothermus marinus. doi:10.1016/j.bbabio.2018.09.205. [PubMan] : Zickermann, V., Parey, K., Brandt, U., Kühlbrandt, W., Mills, D., Siegmund, K., Vonck, J., & Xie, H. (2018). The cryo EM structure of respiratory complex I from Yarrowia lipolytica. Budapest, Hungary. doi:10.1016/j.bbabio.2018.09.133. [PubMan] : Hahn, A., Vonck, J., Mills, D. J., Meier, T., & Kühlbrandt, W. (2018). Structure, mechanism, and regulation of the chloroplast ATP synthase. Science, 360(6389), 1-10. doi:10.1126/science.aat4318. [PubMan] : Klusch, N., Murphy, B. J., Mills, D., Yildiy, Ö., & Kühlbrandt, W. (2017). Structural basis of proton translocation and force generation in mitochondrial ATP synthase. eLife, 6: e33274. doi:10.7554/eLife.33274. [PubMan] : Bausewein, T., Mills, D. J., Langer, J. D., Nitschke, B., Nussberger, S., & Kühlbrandt, W. (2017). Cryo-EM Structure of the TOM Core Complex from Neurospora crassa. Cell, 170(4), 693-700. doi:10.1016/j.cell.2017.07.012. [PubMan] : van Pee, K., Neuhaus, A., D'Imprima, E., Mills, D. J., Kühlbrandt, W., & Yildiz, Ö. (2017). CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin. eLife, 6: e23644. doi:10.7554/eLife.23644.001. [PubMan] : Kohler, R., Mooney, R. A., Mills, D. J., Landick, R., & Cramer, P. (2017). Architecture of a transcribing-translating expressome. Science, 356, 194-197. doi:10.1126/science.aal3059. [PubMan] : Diskowski, M., Mehdipour, A. R., Wunnicke, D., Mills, D. J., Mikusevic, V., Bärland, N., Hoffmann, J., Morgner, N., Steinhoff, H.-J., & Hummer, G. (2017). Helical jackknives control the gates of the double-pore K+ uptake system KtrABs. eLife, 1-21. doi:10.7554/eLife.24303. [PubMan] : Vonck, J., & Mills, D. J. (2017). Advances in high-resolution cryo-EM of oligomeric enzymes. Current Opinion in Structural Biology, 46, 48-54. doi:10.1016/j.sbi.2017.05.016. [PubMan]