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Updated: Jul 16, 2026

Fundamental Technical Elements of Freeze-fracture/Freeze-etch in Biological Electron Microscopy
Published on: September 11, 2014
The molecular architecture of axonemes revealed by cryoelectron tomography
Daniela Nicastro1, Cindi Schwartz, Jason Pierson
1Laboratory for 3D Electron Microscopy of Cells, Department of Molecular, Cellular, and Developmental Biology, CB 347, University of Colorado, Boulder, CO 80309-0347, USA. nicastro@colorado.edu
Abstract:
Eukaryotic flagella and cilia are built on a 9 + 2 array of microtubules plus >250 accessory proteins, forming a biological machine called the axoneme. Here we describe the three-dimensional structure of rapidly frozen axonemes from Chlamydomonas and sea urchin sperm, using cryoelectron tomography and image processing to focus on the motor enzyme dynein. Our images suggest a model for the way dynein generates force to slide microtubules. They also reveal two dynein linkers that may provide "hard-wiring" to coordinate motor enzyme action, both circumferentially and along the axoneme. Periodic densities were also observed inside doublet microtubules; these may contribute to doublet stability.
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