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TitleElectron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM.
Journal, issue, pagesNat Methods, Vol. 10, Issue 6, Page 584-590, Year 2013
Publish dateMay 5, 2013
AuthorsXueming Li / Paul Mooney / Shawn Zheng / Christopher R Booth / Michael B Braunfeld / Sander Gubbens / David A Agard / Yifan Cheng /
PubMed AbstractIn recent work with large high-symmetry viruses, single-particle electron cryomicroscopy (cryo-EM) has achieved the determination of near-atomic-resolution structures by allowing direct fitting of ...In recent work with large high-symmetry viruses, single-particle electron cryomicroscopy (cryo-EM) has achieved the determination of near-atomic-resolution structures by allowing direct fitting of atomic models into experimental density maps. However, achieving this goal with smaller particles of lower symmetry remains challenging. Using a newly developed single electron-counting detector, we confirmed that electron beam-induced motion substantially degrades resolution, and we showed that the combination of rapid readout and nearly noiseless electron counting allow image blurring to be corrected to subpixel accuracy, restoring intrinsic image information to high resolution (Thon rings visible to ∼3 Å). Using this approach, we determined a 3.3-Å-resolution structure of an ∼700-kDa protein with D7 symmetry, the Thermoplasma acidophilum 20S proteasome, showing clear side-chain density. Our method greatly enhances image quality and data acquisition efficiency-key bottlenecks in applying near-atomic-resolution cryo-EM to a broad range of protein samples.
External linksNat Methods / PubMed:23644547 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

5623

3j9i

EMDB-5623: 3D reconstruction of archaeal 20S proteasome
PDB-3j9i: Thermoplasma acidophilum 20S proteasome
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • thermoplasma acidophilum (acidophilic)
KeywordsHYDROLASE / proteasome

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