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Journal Article

Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography

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Medalia,  O.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Weber,  I.
Gerisch, Günther / Cell Dynamics, Max Planck Institute of Biochemistry, Max Planck Society;

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Frangakis,  A. S.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Nicastro,  D.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Gerisch,  G.
Gerisch, Günther / Cell Dynamics, Max Planck Institute of Biochemistry, Max Planck Society;

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Baumeister,  W.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Medalia, O., Weber, I., Frangakis, A. S., Nicastro, D., Gerisch, G., & Baumeister, W. (2002). Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science, 298(5596), 1209-1213.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-6DEE-4
Abstract
Electron tomography of vitrifed cells is a noninvasive three- dimensional imaging technique that opens up new vistas for exploring the supramolecular organization of the cytoplasm. We applied this technique to Dictyostelium cells, focusing on the actin cytoskeleton. In actin networks reconstructed without prior removal of membranes or extraction of soluble proteins, the cross-linking of individual micro laments, their branching angles, and membrane attachment sites can be analyzed. At a resolution of 5 to 6 nanometers, single macromolecules with distinct shapes, such as the 26S proteasome, can be identified in an unperturbed cellular environment.