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IPET and FETR: Experimental Approach for Studying Molecular Structure Dynamics by Cryo-Electron Tomography of a Single-Molecule Structure

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  • Lei Zhang
  • Gang Ren

Abstract

The dynamic personalities and structural heterogeneity of proteins are essential for proper functioning. Structural determination of dynamic/heterogeneous proteins is limited by conventional approaches of X-ray and electron microscopy (EM) of single-particle reconstruction that require an average from thousands to millions different molecules. Cryo-electron tomography (cryoET) is an approach to determine three-dimensional (3D) reconstruction of a single and unique biological object such as bacteria and cells, by imaging the object from a series of tilting angles. However, cconventional reconstruction methods use large-size whole-micrographs that are limited by reconstruction resolution (lower than 20 Å), especially for small and low-symmetric molecule (

Suggested Citation

  • Lei Zhang & Gang Ren, 2012. "IPET and FETR: Experimental Approach for Studying Molecular Structure Dynamics by Cryo-Electron Tomography of a Single-Molecule Structure," PLOS ONE, Public Library of Science, vol. 7(1), pages 1-19, January.
    • Handle: RePEc:plo:pone00:0030249
    DOI: 10.1371/journal.pone.0030249
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    References listed on IDEAS

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    1. Jun Liu & Alberto Bartesaghi & Mario J. Borgnia & Guillermo Sapiro & Sriram Subramaniam, 2008. "Molecular architecture of native HIV-1 gp120 trimers," Nature, Nature, vol. 455(7209), pages 109-113, September.
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    Cited by:

    1. Lingli Kong & Jianfang Liu & Meng Zhang & Zhuoyang Lu & Han Xue & Amy Ren & Jiankang Liu & Jinping Li & Wai Li Ling & Gang Ren, 2023. "Facile hermetic TEM grid preparation for molecular imaging of hydrated biological samples at room temperature," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Jianfang Liu & Ewan K. S. McRae & Meng Zhang & Cody Geary & Ebbe Sloth Andersen & Gang Ren, 2024. "Non-averaged single-molecule tertiary structures reveal RNA self-folding through individual-particle cryo-electron tomography," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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