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Rapid structural analysis of bacterial ribosomes in situ.

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Název: Rapid structural analysis of bacterial ribosomes in situ.
Autoři: Powell, Barrett M., Brant, Tyler S., Davis, Joseph H., Mosalaganti, Shyamal
Zdroj: Communications Biology; 1/28/2025, Vol. 8 Issue 1, p1-9, 9p
Témata: ESCHERICHIA coli, CELL analysis, PROTEIN analysis, INTEGRATED software, ELECTRONIC data processing
Abstrakt: Rapid structural analysis of purified proteins and their complexes has become increasingly common thanks to key methodological advances in cryo-electron microscopy (cryo-EM) and associated data processing software packages. In contrast, analogous structural analysis in cells via cryo-electron tomography (cryo-ET) remains challenging due to critical technical bottlenecks, including low-throughput sample preparation and imaging, and laborious data processing methods. Here, we describe a rapid in situ cryo-ET sample preparation and data analysis workflow that results in the routine determination of sub-nm resolution ribosomal structures. We apply this workflow to E. coli, producing a 5.8 Å structure of the 70S ribosome from cells in less than 10 days and facilitating the discovery of a minor population of 100S-like disomes. We envision our approach to be widely applicable to related bacterial samples. A workflow for rapid cryo-ET structural characterization of bacterial ribosomes in situ and the identification of a 100S-like disome structure. [ABSTRACT FROM AUTHOR]
Copyright of Communications Biology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Rapid structural analysis of bacterial ribosomes in situ.
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  Data: Communications Biology; 1/28/2025, Vol. 8 Issue 1, p1-9, 9p
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  Data: <searchLink fieldCode="DE" term="%22ESCHERICHIA+coli%22">ESCHERICHIA coli</searchLink><br /><searchLink fieldCode="DE" term="%22CELL+analysis%22">CELL analysis</searchLink><br /><searchLink fieldCode="DE" term="%22PROTEIN+analysis%22">PROTEIN analysis</searchLink><br /><searchLink fieldCode="DE" term="%22INTEGRATED+software%22">INTEGRATED software</searchLink><br /><searchLink fieldCode="DE" term="%22ELECTRONIC+data+processing%22">ELECTRONIC data processing</searchLink>
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  Data: Rapid structural analysis of purified proteins and their complexes has become increasingly common thanks to key methodological advances in cryo-electron microscopy (cryo-EM) and associated data processing software packages. In contrast, analogous structural analysis in cells via cryo-electron tomography (cryo-ET) remains challenging due to critical technical bottlenecks, including low-throughput sample preparation and imaging, and laborious data processing methods. Here, we describe a rapid in situ cryo-ET sample preparation and data analysis workflow that results in the routine determination of sub-nm resolution ribosomal structures. We apply this workflow to E. coli, producing a 5.8 Å structure of the 70S ribosome from cells in less than 10 days and facilitating the discovery of a minor population of 100S-like disomes. We envision our approach to be widely applicable to related bacterial samples. A workflow for rapid cryo-ET structural characterization of bacterial ribosomes in situ and the identification of a 100S-like disome structure. [ABSTRACT FROM AUTHOR]
– Name: Abstract
  Label:
  Group: Ab
  Data: <i>Copyright of Communications Biology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1038/s42003-025-07586-y
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              Text: 1/28/2025
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