Abstract
In the last years the atomic force microscope (AFM; ref. 1) has become a powerful imaging tool for the biologist. The unique features like the possibility to image biological structures in their native environment (i.e., in buffer solution, at room temperature, and under normal pressure), the high lateral and vertical resolution, and the high signal-to-noise ratio of the topographs acquired by AFM make this instrument outstanding. It has made the observation of different single biomolecules at work and the monitoring of biomolecular interactions by time-lapse AFM possible (for recent reviews, see refs. 2–4).
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References
Binnig, G., Quate, C. F., and Gerber, C. (1986) Atomic force microscope. Phys. Rev. Lett. 56, 930–933.
Engel, A., Lyubchenko, Y., and Müller, D. J. (1999) Atomic force microscopy: A powerful tool to observe biomolecules at work. Trends Cell Biol. 9, 77–80.
Stolz, M., Stoffler, D., Aebi, U., and Goldsbury, C. (2000) Monitoring biomolecular interactions by time-lapse atomic force microscopy. J. Struct. Biol. 131, 171–180.
Engel, A. and Müller, D. J. (2000) Observing single biomolecules at work with the atomic force microscope. Nat. Struct. Biol. 7, 715–718.
Stahlberg, H., Fotiadis, D., Scheuring, S., Rémigy, H., Braun, T., Mitsuoka, K., et al. (2001) Two-dimensional crystals: A powerful approach to assess structure, function and dynamics of membrane proteins. FEBS Lett. 504, 166–172.
Zhong, Q., Inniss, D., Kjoller, K., and Elings, V. B. (1993) Fractured polymer/silica fiber surface studied by tapping mode atomic force microscopy. Surf. Sci. Lett. 290, L688–L692.
Putman, C. A. J., Vanderwerf, K. O., de Grooth, B. G., Vanhulst, N. F., and Greve, J. (1994) Tapping mode atomic-force microscopy in liquid. Appl. Phys. Lett. 64, 2454–2456.
Hansma, P. K., Cleveland, J. P., Radmacher, M., Walters, D. A., Hillner, P. E., Bezanilla, M., et al. (1994) Tapping mode atomic force microscopy in liquids. Appl. Phys. Lett. 64, 1738–1740.
Han, W. H., Lindsay, S. M., and Jing, T. W. (1996) A magnetically driven oscillating probe microscope for operation in liquids. Appl. Phys. Lett. 69, 4111–4113.
Han, W. H., Lindsay, S. M., Dlakic, M., and Harrington, R. E. (1997) Kinked DNA. Nature 386, 563.
Müller, D. J., Fotiadis, D., Scheuring, S., Müller, S. A., and Engel, A. (1999) Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope. Biophys. J. 76, 1101–1111.
Fotiadis, D., Scheuring, S., Müller, S. A., Engel, A., and Müller, D. J. (2002) Imaging and manipulation of biological structures with the AFM. Micron 33, 385–397.
Oesterhelt, D. and Stoeckenius, W. (1973) Functions of a new photoreceptor membrane. Proc. Natl Acad. Sci. USA 70, 2853–2857.
Oesterhelt, D. and Stoeckenius, W. (1971) Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat. New Biol. 233, 149–152.
Lanyi, J. K. (1993) Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta 1183, 241–261.
Khorana, H. G. (1988) Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J. Biol. Chem. 263, 7439–7442.
Blaurock, A. E. and Stoeckenius, W. (1971) Structure of the purple membrane. Nat. New Biol. 233, 152–155.
Lanyi, J. K. and Luecke, H. (2001) Bacteriorhodopsin. Curr. Opin. Struct. Biol. 11, 415–419.
Heymann, J. B., Müller, D. J., Landau, E. M., Rosenbusch, J. P., Pebay-Peyroula, E., Büldt, G., et al. (1999) Charting the surfaces of the purple membrane. J. Struct. Biol. 128, 243–249.
Müller, D. J., Schoenenberger, C.-A., Büldt, G., and Engel, A. (1996) Immunoatomic force microscopy of purple membrane. Biophys. J. 70, 1796–1802.
Müller, D. J., Schabert, F. A., Büldt, G., and Engel, A. (1995) Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy. Biophys. J. 68, 1681–1686.
Müller, D. J. and Engel, A. (1997) The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions. Biophys. J. 73, 1633–1644.
Müller, D. J., Sass, H.-J., Müller, S. A., Büldt, G., and Engel, A. (1999) Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. J. Mol. Biol. 285, 1903–1909.
Müller, D. J., Büldt, G., and Engel, A. (1995) Force-induced conformational change of bacteriorhodopsin. J. Mol. Biol. 249, 239–243.
Misell, D. L. and Brown, E. B. (1987) Electron diffraction: An introduction for biologists, in Practical Methods in Electron Microscopy, vol. 12 (Glauert, A. M., ed.) Elsevier Science Publishers B. V., The Netherlands.
Xu, S. and Arnsdorf, M. F. (1994) Calibration of the scanning (atomic) force microscope with gold particles. J. Microsc. 173, 199–210.
Schwarz, U. D., Haefke, H., Reimann, P., and Güntherodt, H.-J. (1994) Tip artefacts in scanning force microscopy. J. Microsc. 173, 183–197.
Kimura, Y., Vassylyev, D. G., Miyazawa, A., Kidera, A., Matsushima, M., Mitsuoka, K., Murata, K., et al. (1997) Surface of bacteriorhodopsin revealed by high-resolution electron crystallography. Nature 389, 206–211.
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Fotiadis, D., Engel, A. (2004). High-Resolution Imaging of Bacteriorhodopsin by Atomic Force Microscopy. In: Braga, P.C., Ricci, D. (eds) Atomic Force Microscopy. Methods in Molecular Biology™, vol 242. Humana Press. https://doi.org/10.1385/1-59259-647-9:291
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DOI: https://doi.org/10.1385/1-59259-647-9:291
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