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Limiting factors in single particle cryo electron tomography

Modern methods of cryo electron microscopy and tomography allow visualization of protein nanomachines in their native state at the nanometer scale. Image processing methods including sub-volume averaging applied to repeating macromolecular elements within tomograms allow exploring their structures w...

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Detalles Bibliográficos
Autores principales: Kudryashev, Mikhail, Castaño-Díez, Daniel, Stahlberg, Henning
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology (RNCSB) Organization 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962116/
https://www.ncbi.nlm.nih.gov/pubmed/24688638
http://dx.doi.org/10.5936/csbj.201207002
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author Kudryashev, Mikhail
Castaño-Díez, Daniel
Stahlberg, Henning
author_facet Kudryashev, Mikhail
Castaño-Díez, Daniel
Stahlberg, Henning
author_sort Kudryashev, Mikhail
collection PubMed
description Modern methods of cryo electron microscopy and tomography allow visualization of protein nanomachines in their native state at the nanometer scale. Image processing methods including sub-volume averaging applied to repeating macromolecular elements within tomograms allow exploring their structures within the native context of the cell, avoiding the need for protein isolation and purification. Today, many different data acquisition protocols and software solutions are available to researchers to determine average structures of macromolecular complexes and potentially to classify structural intermediates. Here, we list the density maps reported in the literature, and analyze each structure for the chosen instrumental settings, sample conditions, main processing steps, and obtained resolution. We present conclusions that identify factors currently limiting the resolution gained by this approach.
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spelling pubmed-39621162014-03-31 Limiting factors in single particle cryo electron tomography Kudryashev, Mikhail Castaño-Díez, Daniel Stahlberg, Henning Comput Struct Biotechnol J Mini Review Modern methods of cryo electron microscopy and tomography allow visualization of protein nanomachines in their native state at the nanometer scale. Image processing methods including sub-volume averaging applied to repeating macromolecular elements within tomograms allow exploring their structures within the native context of the cell, avoiding the need for protein isolation and purification. Today, many different data acquisition protocols and software solutions are available to researchers to determine average structures of macromolecular complexes and potentially to classify structural intermediates. Here, we list the density maps reported in the literature, and analyze each structure for the chosen instrumental settings, sample conditions, main processing steps, and obtained resolution. We present conclusions that identify factors currently limiting the resolution gained by this approach. Research Network of Computational and Structural Biotechnology (RNCSB) Organization 2012-07-01 /pmc/articles/PMC3962116/ /pubmed/24688638 http://dx.doi.org/10.5936/csbj.201207002 Text en © Kudryashev et al. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly cited.
spellingShingle Mini Review
Kudryashev, Mikhail
Castaño-Díez, Daniel
Stahlberg, Henning
Limiting factors in single particle cryo electron tomography
title Limiting factors in single particle cryo electron tomography
title_full Limiting factors in single particle cryo electron tomography
title_fullStr Limiting factors in single particle cryo electron tomography
title_full_unstemmed Limiting factors in single particle cryo electron tomography
title_short Limiting factors in single particle cryo electron tomography
title_sort limiting factors in single particle cryo electron tomography
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962116/
https://www.ncbi.nlm.nih.gov/pubmed/24688638
http://dx.doi.org/10.5936/csbj.201207002
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