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TitleExperimental evaluation of super-resolution imaging and magnification choice in single-particle cryo-EM.
Journal, issue, pagesJ Struct Biol X, Vol. 5, Page 100047, Year 2021
Publish dateMar 13, 2021
AuthorsJ Ryan Feathers / Katherine A Spoth / J Christopher Fromme /
PubMed AbstractThe resolution of cryo-EM reconstructions is fundamentally limited by the Nyquist frequency, which is half the sampling frequency of the detector and depends upon the magnification used. In ...The resolution of cryo-EM reconstructions is fundamentally limited by the Nyquist frequency, which is half the sampling frequency of the detector and depends upon the magnification used. In principle, super-resolution imaging should enable reconstructions to surpass the physical Nyquist limit by increasing sampling frequency, yet there are few reports of reconstructions that do so. Here we directly examine the contribution of super-resolution information, obtained with the K3 direct electron detector using a 2-condenser microscope, to single-particle cryo-EM reconstructions surpassing the physical Nyquist limit. We also present a comparative analysis of a sample imaged at four different magnifications. This analysis demonstrates that lower magnifications can be beneficial, despite the loss of higher resolution signal, due to the increased number of particle images obtained. To highlight the potential utility of lower magnification data collection, we produced a 3.5 Å reconstruction of jack bean urease with particles from a single micrograph.
External linksJ Struct Biol X / PubMed:33817625 / PubMed Central
MethodsEM (single particle)
Resolution2.77 - 3.84407 Å
Structure data

20016

7kns

EMDB-20016: The cryo-EM structure of Jack bean urease: beyond the physical Nyquist limit using the K3 detector
PDB-7kns: Cryo-EM structure of jack bean urease
Method: EM (single particle) / Resolution: 2.77 Å

EMDB-20213:
The cryo-EM structure of Jack bean urease: further beyond the physical Nyquist limit using the K3 detector
Method: EM (single particle) / Resolution: 3.06 Å

EMDB-20214:
The cryo-EM structure of Jack bean urease: 3D reconstruction from a single exposure
Method: EM (single particle) / Resolution: 3.84407 Å

EMDB-23573:
The cryo-EM structure of Jack bean urease at 63,000 nominal magnification
Method: EM (single particle) / Resolution: 2.86 Å

EMDB-23604:
Jack bean urease at 79,000 nominal magnification
Method: EM (single particle) / Resolution: 2.86 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION / Nickel

ChemComp-PO4:
PHOSPHATE ION / Phosphate

Source
  • canavalia ensiformis (jack bean)
KeywordsHYDROLASE / urease

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