Microtubule structure at 8 Å resolution

Huilin Li, David J. DeRosier, William V. Nicholson, Eva Nogales, Kenneth H. Downing

Research output: Contribution to journalArticle

313 Citations (Scopus)

Abstract

We have obtained a 3D reconstruction of intact microtubules, using cryoelectron microscopy and image processing, at a resolution of about 8 Å, sufficient to resolve much of the secondary structure. The level of detail in the map allows docking of the tubulin structure previously determined by electron crystallography, with very strong constraints, providing several important insights not previously available through docking tubulin into lower-resolution maps. This work provides an improved picture of the interactions between adjacent protofilaments, which are responsible for microtubule stability, and also suggests that some structural features are different in microtubules from those in the zinc sheets with which the tubulin structure was determined.
Original languageEnglish
Pages (from-to)1317-1328
Number of pages12
JournalStructure
Volume10
Issue number10
DOIs
Publication statusPublished - 2002

Keywords

  • TUBULIN
  • microtubules
  • electron crystallography
  • Protein structure
  • dynamic instability

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  • Research Output

    • 313 Citations
    • 1 Poster

    Microtubule structure at 8 Å resolution

    Nicholson, W., 2002, p. 413a.

    Research output: Contribution to conferencePoster

    Cite this

    Li, H., DeRosier, D. J., Nicholson, W. V., Nogales, E., & Downing, K. H. (2002). Microtubule structure at 8 Å resolution. Structure, 10(10), 1317-1328. https://doi.org/10.1016/S0969-2126(02)00827-4