Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Review Article
  • Published:

Conformational changes studied by cryo-electron microscopy

Nature Structural Biology volume 7, pages 711–714 (2000)Cite this article

Abstract

Biological processes involving movement, such as muscle contraction or the opening of an ion channel through a membrane, are mediated through conformational changes. These changes often occur in large and flexible macromolecular complexes. Cryo-electron microscopy provides a means of capturing different conformational states of such assemblies. Even if the resulting density maps are at low resolution, they can be combined with atomic structures of subcomplexes or isolated components determined by X-ray crystallography or NMR. This review presents a brief summary of the principles and recent advances in macromolecular structure determination by cryo-electron microscopy.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Three-dimensional reconstruction of the helical structure of filamentous actin decorated with brush border myosin I in a, rigor (no nucleotide bound) and b, ADP-bound states21.
Figure 2: End views of the open rings of GroEL–GroES chaperonin complexes in a, ATP and b, ADP states16.
Figure 3: The transmembrane region of the nicotinic acetylcholine receptor, reconstructed at 9 Å from helically ordered membrane tubes26.
Figure 4: The perfringolysin structure29 in a, the soluble monomeric form and b, fitted into a cryo-EM density envelope (blue outline) of a helical oligomeric form of pneumolysin30.

Similar content being viewed by others

References

  1. Dubochet, J., et al. Quart. Rev. Biophys. 21, 129–228 (1988).

    Article  CAS  Google Scholar 

  2. DeRosier, D.J. & Klug, A. Nature 217, 130–134 (1968).

    Article  CAS  Google Scholar 

  3. Amos, L.A., Henderson, R. & Unwin, P.N.T. Prog. Biophys. Mol. Biol. 39, 183–231 (1982).

    Article  CAS  PubMed Central  Google Scholar 

  4. Radermacher, M., Wagenknecht, T., Verschoor, A. & Frank, J. J. Microsc. 146, 113–136 (1987).

    Article  CAS  PubMed Central  Google Scholar 

  5. Crowther, R.A. Phil. Trans. Roy. Soc. Lond. 261, 221–230 (1971).

    Article  CAS  Google Scholar 

  6. van Heel, M. Ultramicrosc. 21, 95–100; 111–124 (1987).

    Article  Google Scholar 

  7. Henderson, R. Quart. Rev. Biophys. 28, 171–193 (1995).

    Article  CAS  Google Scholar 

  8. Orlova, E.V. et al. Nature Struct. Biol. 7, 48–53 (2000).

    Article  CAS  PubMed Central  Google Scholar 

  9. Henderson, R. et al. J. Mol. Biol. 213, 899–929 (1990).

    Article  CAS  Google Scholar 

  10. Böttcher, B., Wynne, S.A. & Crowther, R.A. Nature 386, 88–91 (1997).

    Article  PubMed Central  Google Scholar 

  11. Conway, J.F. et al. Nature 386, 91–94 (1997).

    Article  CAS  PubMed Central  Google Scholar 

  12. Matadeen, R., et al. Structure 7, 1575–1583 (1999).

    Article  CAS  PubMed Central  Google Scholar 

  13. Gabashvili, I.S., et al. Cell 100, 537–549 (2000).

    Article  CAS  PubMed Central  Google Scholar 

  14. Berriman, J. & Unwin, N. Ultramicrosc. 56, 241–252 (1994).

    Article  CAS  Google Scholar 

  15. White, H.D., Walker, M.L. & Trinick, J. J. Struct. Biol. 121, 306–313 (1998).

    Article  CAS  PubMed Central  Google Scholar 

  16. Rye, H.S., et al. Cell 97, 325–338 (1999).

    Article  CAS  PubMed Central  Google Scholar 

  17. Schoehn, G., Quaite-Randall, E., Jiménez, J.L., Joachimiak, A. & Saibil, H.R. J. Mol. Biol. 296, 813–819 (2000).

    Article  CAS  PubMed Central  Google Scholar 

  18. Olson, N.H., et al. Proc. Natl. Acad. Sci. USA 90, 507–511 (1993).

    Article  CAS  PubMed Central  Google Scholar 

  19. Wriggers, W., Milligan, R.A. & McCammon, J.A. J. Struct. Biol. 125, 185–195 (1999).

    Article  CAS  PubMed Central  Google Scholar 

  20. Volkmann, N. & Hanein, D. J. Struct. Biol. 125, 176–184 (1999).

    Article  CAS  PubMed Central  Google Scholar 

  21. Jontes, J.D. & Milligan, R.A. J. Cell Biol. 139, 683–693 (1997).

    Article  CAS  PubMed Central  Google Scholar 

  22. Stark, H., et al. Cell 88, 18–28 (1997).

    Article  Google Scholar 

  23. Frank, J. & Agrawal, R.K., Nature 406, 318–322 (2000).

    Article  CAS  PubMed Central  Google Scholar 

  24. Roseman, A.M., Chen, S., White, H., Braig, K. & Saibil, H.R. Cell 87, 241–251 (1996).

    Article  CAS  PubMed Central  Google Scholar 

  25. Xu, Z., Horwich, A.L. & Sigler, P.B. Nature 388, 741–750 (1997).

    Article  CAS  PubMed Central  Google Scholar 

  26. Unwin, N. Nature 373, 37–43 (1995).

    Article  CAS  Google Scholar 

  27. Miyazawa, A., Fujiyoshi, Y., Stowell, M. & Unwin, N. J. Mol. Biol. 288, 765–786 (1999).

    Article  CAS  Google Scholar 

  28. Fuller, S.D., Berriman, J.A., Butcher, S.J. & Gowen, B.E. Cell 81, 715–725 (1995).

    Article  CAS  PubMed Central  Google Scholar 

  29. Rossjohn, J., Feil, S.C., McKinstry, W.J., Tweten, R.K. & Parker, M.W. Cell 89, 685–692 (1997).

    Article  CAS  PubMed Central  Google Scholar 

  30. Gilbert, R.J.C., et al. Cell 97, 647–655 (1999).

    Article  CAS  Google Scholar 

  31. Frank, J. Three-dimensional electron microscopy of macromolecular assemblies. (Academic Press, San Diego; 1996).

    Google Scholar 

Download references

Acknowledgements

I am grateful to S. Fuller for comments on the manuscript.

Author information

Authors and Affiliations

  1. Crystallography Department, Birkbeck College, Malet Street, London, WC1E 7HX, UK

    Helen R. Saibil

Authors
  1. Helen R. Saibil
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Helen R. Saibil.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Saibil, H. Conformational changes studied by cryo-electron microscopy. Nat Struct Mol Biol 7, 711–714 (2000). https://doi.org/10.1038/78923

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/78923

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing