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TitleBeam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 1957, Year 2021
Publish dateMar 30, 2021
AuthorsJonathan Bouvette / Hsuan-Fu Liu / Xiaochen Du / Ye Zhou / Andrew P Sikkema / Juliana da Fonseca Rezende E Mello / Bradley P Klemm / Rick Huang / Roel M Schaaper / Mario J Borgnia / Alberto Bartesaghi /
PubMed AbstractTomographic reconstruction of cryopreserved specimens imaged in an electron microscope followed by extraction and averaging of sub-volumes has been successfully used to derive atomic models of ...Tomographic reconstruction of cryopreserved specimens imaged in an electron microscope followed by extraction and averaging of sub-volumes has been successfully used to derive atomic models of macromolecules in their biological environment. Eliminating biochemical isolation steps required by other techniques, this method opens up the cell to in-situ structural studies. However, the need to compensate for errors in targeting introduced during mechanical navigation of the specimen significantly slows down tomographic data collection thus limiting its practical value. Here, we introduce protocols for tilt-series acquisition and processing that accelerate data collection speed by up to an order of magnitude and improve map resolution compared to existing approaches. We achieve this by using beam-image shift to multiply the number of areas imaged at each stage position, by integrating geometrical constraints during imaging to achieve high precision targeting, and by performing per-tilt astigmatic CTF estimation and data-driven exposure weighting to improve final map resolution. We validated our beam image-shift electron cryo-tomography (BISECT) approach by determining the structure of a low molecular weight target (~300 kDa) at 3.6 Å resolution where density for individual side chains is clearly resolved.
External linksNat Commun / PubMed:33785757 / PubMed Central
MethodsEM (single particle) / EM (subtomogram averaging)
Resolution3.3 - 5.6 Å
Structure data

EMDB-23355:
Structure of dNTPase at 3.3 Angstrom Resolution
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-23356:
Structure of dNTPase at 3.6 Angstrom Resolution
Method: EM (subtomogram averaging) / Resolution: 3.6 Å

EMDB-23357:
Structure of 80S ribosome from EMPIAR-10064 at 5.6 Angstrom Resolution
Method: EM (subtomogram averaging) / Resolution: 5.6 Å

EMDB-23358:
Structure of E. coli 70S ribosome from EMPIAR-10304 at 4.8 Angstrom Resolution
Method: EM (subtomogram averaging) / Resolution: 4.8 Å

Source
  • Vibrio cholerae (bacteria)
  • Oryctolagus cuniculus (rabbit)
  • Escherichia coli (E. coli)
KeywordsAlgorithms / Cryoelectron Microscopy / Electron Microscope Tomography / Image Processing, Computer-Assisted / Imaging, Three-Dimensional / Macromolecular Substances / Particle Size / Reproducibility of Results / Tomography, X-Ray Computed

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