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  In Situ Cryo-Electron Tomography: A Post-Reductionist Approach to Structural Biology

Asano, S., Engel, B. D., & Baumeister, W. (2016). In Situ Cryo-Electron Tomography: A Post-Reductionist Approach to Structural Biology. Journal of Molecular Biology (London), 428(2, Part A. Special Issue: Study of biomolecules and biological systems: Proteins), 332-343. doi:10.1016/j.jmb.2015.09.030.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-266C-A Version Permalink: http://hdl.handle.net/21.11116/0000-0004-57FA-1
Genre: Journal Article

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 Creators:
Asano, Shoh1, Author              
Engel, Benjamin D.1, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: TRANSMISSION ELECTRON-MICROSCOPY; PARTICLE CRYO-EM; 26S PROTEASOME; RADIATION-DAMAGE; SAMPLE PREPARATION; VITREOUS SECTIONS; INTACT-CELLS; MOLECULAR ARCHITECTURE; ANGSTROM RESOLUTION; SPATIAL PRECISIONcryo-EM; tomography; template matching; visual proteomics; subtomogram averaging;
 Abstract: Cryo-electron tomography is a powerful technique that can faithfully image the native cellular environment at nanometer resolution. Unlike many other imaging approaches, cryo-electron tomography provides a label-free method of detecting biological structures, relying on the intrinsic contrast of frozen cellular material for direct identification of macromolecules. Recent advances in sample preparation, detector technology, and phase plate imaging have enabled the structural characterization of protein complexes within intact cells. Here, we review these technical developments and outline a detailed computational workflow for in situ structural analysis. Two recent studies are described to illustrate how this workflow can be adapted to examine both known and unknown cellular complexes. The stage is now set to realize the promise of visual proteomics a complete structural description of the cell's native molecular landscape. (C) 2015 Elsevier Ltd. All rights reserved.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000370833000009
DOI: 10.1016/j.jmb.2015.09.030
 Degree: -

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Project name : ERC-2012-SyG_318987-ToPAG
Grant ID : 318987
Funding program : -
Funding organization : European Commission

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 428 (2, Part A. Special Issue: Study of biomolecules and biological systems: Proteins) Sequence Number: - Start / End Page: 332 - 343 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042