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3. The application of Graphene as a sample support in Transmission Electron Microscopy

Author

Pantelic, R. S., Meyer, J. C., Kaiser, U., and Stahlberg, H.

Subjects
Physics - Biological Physics, Condensed Matter - Materials Science
Abstract

Transmission electron microscopy has witnessed rampant development and surging point resolution over the past few years. The improved imaging performance of modern electron microscopes shifts the bottleneck for image contrast and resolution to sample preparation. Hence, it is increasingly being realized that the full potential of electron microscopy will only be realized with the optimization of current sample preparation techniques. Perhaps the most recognized issues are background signal and noise contributed by sample supports, sample charging and instability. Graphene provides supports of single atom thickness, extreme physical stability, periodic structure, and ballistic electrical conductivity. As an increasing number of applications adapting graphene to their benefit emerge, we discuss the unique capabilities afforded by the use of graphene as a sample support for electron microscopy., Comment: Review, to appear in solid state communications

Published
2012
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4. Vanadate-trapped BSEP in nanodiscs

Author

Liu, H., primary, Irobalieva, R.N., additional, Kowal, J., additional, Ni, D., additional, Nosol, K., additional, Bang-Sorensen, R., additional, Lancien, L., additional, Stahlberg, H., additional, Stieger, B., additional, and Locher, K.P., additional

Published
2023
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6. Nucleotide-bound BSEP in nanodiscs

Author

Liu, H., primary, Irobalieva, R.N., additional, Kowal, J., additional, Ni, D., additional, Nosol, K., additional, Bang-Sorensen, R., additional, Lancien, L., additional, Stahlberg, H., additional, Stieger, B., additional, and Locher, K.P., additional

Published
2023
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17. Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies (MBPs have not been built de novo)

Author

Botte, M., primary, Ni, D., additional, Schenck, S., additional, Zimmermann, I., additional, Chami, M., additional, Bocquet, N., additional, Egloff, P., additional, Bucher, D., additional, Trabuco, M., additional, Cheng, R.K.Y., additional, Brunner, J.D., additional, Seeger, M.A., additional, Stahlberg, H., additional, and Hennig, M., additional

Published
2022
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18. Crystal structure of ProMacrobody 21 with bound maltose

Author

Botte, M., primary, Ni, D., additional, Schenck, S., additional, Zimmermann, I., additional, Chami, M., additional, Bocquet, N., additional, Egloff, P., additional, Bucher, D., additional, Trabuco, M., additional, Cheng, R.K.Y., additional, Brunner, J.D., additional, Seeger, M.A., additional, Stahlberg, H., additional, and Hennig, M., additional

Published
2022
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23. Human TRPV4 structure in presence of 4a-PDD

Author

Botte, M., primary, Ulrich, A.K.G., additional, Adaixo, R., additional, Gnutt, D., additional, Brockmann, A., additional, Bucher, D., additional, Chami, M., additional, Bocquet, M., additional, Ebbinghaus-Kintscher, U., additional, Puetter, V., additional, Becker, A., additional, Egner, U., additional, Stahlberg, H., additional, Hennig, M., additional, and Holton, S.J., additional

Published
2021
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24. ABCG2 topotecan turnover-1 state

Author

Yu, Q., primary, Ni, D., additional, Kowal, J., additional, Manolaridis, I., additional, Jackson, S.M., additional, Stahlberg, H., additional, and Locher, K.P., additional

Published
2021
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25. ABCG2 E1S turnover-2 state

Author

Ni, D., primary, Yu, Q., additional, Kowal, J., additional, Manolaridis, I., additional, Jackson, S.M., additional, Stahlberg, H., additional, and Locher, K.P., additional

Published
2021
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26. ABCG2 topotecan turnover-2 state

Author

Yu, Q., primary, Ni, D., additional, Kowal, J., additional, Manolaridis, I., additional, Jackson, S.M., additional, Stahlberg, H., additional, and Locher, K.P., additional

Published
2021
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30. Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice

Author

Ruskamo, S. (Salla), Krokengen, O. C. (Oda C.), Kowal, J. (Julia), Nieminen, T. (Tuomo), Lehtimäki, M. (Mari), Raasakka, A. (Arne), Dandey, V. P. (Venkata P.), Vattulainen, I. (Ilpo), Stahlberg, H. (Henning), Kursula, P. (Petri), Ruskamo, S. (Salla), Krokengen, O. C. (Oda C.), Kowal, J. (Julia), Nieminen, T. (Tuomo), Lehtimäki, M. (Mari), Raasakka, A. (Arne), Dandey, V. P. (Venkata P.), Vattulainen, I. (Ilpo), Stahlberg, H. (Henning), and Kursula, P. (Petri)

Abstract

Myelin protein P2 is a peripheral membrane protein of the fatty acid–binding protein family that functions in the formation and maintenance of the peripheral nerve myelin sheath. Several P2 gene mutations cause human Charcot-Marie-Tooth neuropathy, but the mature myelin sheath assembly mechanism is unclear. Here, cryo-EM of myelin-like proteolipid multilayers revealed an ordered three-dimensional (3D) lattice of P2 molecules between stacked lipid bilayers, visualizing supramolecular assembly at the myelin major dense line. The data disclosed that a single P2 layer is inserted between two bilayers in a tight intermembrane space of ∼3 nm, implying direct interactions between P2 and two membrane surfaces. X-ray diffraction from P2-stacked bicelle multilayers revealed lateral protein organization, and surface mutagenesis of P2 coupled with structure-function experiments revealed a role for both the portal region of P2 and its opposite face in membrane interactions. Atomistic molecular dynamics simulations of P2 on model membrane surfaces suggested that Arg-88 is critical for P2-membrane interactions, in addition to the helical lid domain. Negatively charged lipid headgroups stably anchored P2 on the myelin-like bilayer surface. Membrane binding may be accompanied by opening of the P2 β-barrel structure and ligand exchange with the apposing bilayer. Our results provide an unprecedented view into an ordered, multilayered biomolecular membrane system induced by the presence of a peripheral membrane protein from human myelin. This is an important step toward deciphering the 3D assembly of a mature myelin sheath at the molecular level.

Published
2020

36. Molecular structure and function of myelin protein P0 in membrane stacking

Author

Raasakka, A. (Arne), Ruskamo, S. (Salla), Kowal, J. (Julia), Han, H. (Huijong), Baumann, A. (Anne), Myllykoski, M. (Matti), Fasano, A. (Anna), Rossano, R. (Rocco), Riccio, P. (Paolo), Bürck, J. (Jochen), Ulrich, A. S. (Anne S.), Stahlberg, H. (Henning), Kursula, P. (Petri), Raasakka, A. (Arne), Ruskamo, S. (Salla), Kowal, J. (Julia), Han, H. (Huijong), Baumann, A. (Anne), Myllykoski, M. (Matti), Fasano, A. (Anna), Rossano, R. (Rocco), Riccio, P. (Paolo), Bürck, J. (Jochen), Ulrich, A. S. (Anne S.), Stahlberg, H. (Henning), and Kursula, P. (Petri)

Abstract

Compact myelin forms the basis of nerve insulation essential for higher vertebrates. Dozens of myelin membrane bilayers undergo tight stacking, and in the peripheral nervous system, this is partially enabled by myelin protein zero (P0). Consisting of an immunoglobulin (Ig)-like extracellular domain, a single transmembrane helix, and a cytoplasmic extension (P0ct), P0 harbours an important task in ensuring the integrity of compact myelin in the extracellular compartment, referred to as the intraperiod line. Several disease mutations resulting in peripheral neuropathies have been identified for P0, reflecting its physiological importance, but the arrangement of P0 within the myelin ultrastructure remains obscure. We performed a biophysical characterization of recombinant P0ct. P0ct contributes to the binding affinity between apposed cytoplasmic myelin membrane leaflets, which not only results in changes of the bilayer properties, but also potentially involves the arrangement of the Ig-like domains in a manner that stabilizes the intraperiod line. Transmission electron cryomicroscopy of native full-length P0 showed that P0 stacks lipid membranes by forming antiparallel dimers between the extracellular Ig-like domains. The zipper-like arrangement of the P0 extracellular domains between two membranes explains the double structure of the myelin intraperiod line. Our results contribute to the understanding of PNS myelin, the role of P0 therein, and the underlying molecular foundation of compact myelin stability in health and disease.

Published
2019

39. Rhodopsin-Gi protein complex

Author

Tsai, C.-J., primary, Marino, J., additional, Adaixo, R.J., additional, Pamula, F., additional, Muehle, J., additional, Maeda, S., additional, Flock, T., additional, Taylor, N.M.I., additional, Mohammed, I., additional, Matile, H., additional, Dawson, R.J.P., additional, Deupi, X., additional, Stahlberg, H., additional, and Schertler, G.F.X., additional

Published
2019
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40. Endogeneous native human 20S proteasome

Author

Schmidli, C., primary, Albiez, S., additional, Rima, L., additional, Righetto, R., additional, Mohammed, I., additional, Oliva, P., additional, Kovacik, L., additional, Stahlberg, H., additional, and Braun, T., additional

Published
2019
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41. Tobacco Mosaic Virus (TMV)

Author

Schmidli, C., primary, Albiez, S., additional, Rima, L., additional, Righetto, R., additional, Mohammed, I., additional, Oliva, P., additional, Kovacik, L., additional, Stahlberg, H., additional, and Braun, T., additional

Published
2019
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