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TitleHigh-resolution cryo-EM using beam-image shift at 200 keV.
Journal, issue, pagesIUCrJ, Vol. 7, Issue Pt 6, Page 1179-1187, Year 2020
Publish dateNov 1, 2020
AuthorsJennifer N Cash / Sarah Kearns / Yilai Li / Michael A Cianfrocco /
PubMed AbstractRecent advances in single-particle cryo-electron microscopy (cryo-EM) data collection utilize beam-image shift to improve throughput. Despite implementation on 300 keV cryo-EM instruments, it ...Recent advances in single-particle cryo-electron microscopy (cryo-EM) data collection utilize beam-image shift to improve throughput. Despite implementation on 300 keV cryo-EM instruments, it remains unknown how well beam-image-shift data collection affects data quality on 200 keV instruments and the extent to which aberrations can be computationally corrected. To test this, a cryo-EM data set for aldolase was collected at 200 keV using beam-image shift and analyzed. This analysis shows that the instrument beam tilt and particle motion initially limited the resolution to 4.9 Å. After particle polishing and iterative rounds of aberration correction in , a 2.8 Å resolution structure could be obtained. This analysis demonstrates that software correction of microscope aberrations can provide a significant improvement in resolution at 200 keV.
External linksIUCrJ / PubMed:33209328 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 4.9 Å
Structure data

22754

7k9l

EMDB-22754, PDB-7k9l:
Aldolase, rabbit muscle (no beam-tilt refinement)
Method: EM (single particle) / Resolution: 4.9 Å

22755

7k9x

EMDB-22755, PDB-7k9x:
Aldolase, rabbit muscle (beam-tilt refinement x1)
Method: EM (single particle) / Resolution: 3.8 Å

22756

7ka2

EMDB-22756, PDB-7ka2:
Aldolase, rabbit muscle (beam-tilt refinement x2)
Method: EM (single particle) / Resolution: 3.6 Å

22757

7ka3

EMDB-22757, PDB-7ka3:
Aldolase, rabbit muscle (beam-tilt refinement x3)
Method: EM (single particle) / Resolution: 3.3 Å

22758

7ka4

EMDB-22758, PDB-7ka4:
Aldolase, rabbit muscle (beam-tilt refinement x4)
Method: EM (single particle) / Resolution: 2.8 Å

Source
  • oryctolagus cuniculus (rabbit)
KeywordsLYASE / glycolysis / gluconeogenesis / Carbohydrate degradation / Homotetramer

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