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TitleRefined Cryo-EM Structure of the T4 Tail Tube: Exploring the Lowest Dose Limit.
Journal, issue, pagesStructure, Vol. 25, Issue 9, Page 1436-11441.e2, Year 2017
Publish dateSep 5, 2017
AuthorsWeili Zheng / Fengbin Wang / Nicholas M I Taylor / Ricardo C Guerrero-Ferreira / Petr G Leiman / Edward H Egelman /
PubMed AbstractThe bacteriophage T4 contractile tail (containing a tube and sheath) was the first biological assembly reconstructed in three dimensions by electron microscopy at a resolution of ∼35 Å in 1968. A ...The bacteriophage T4 contractile tail (containing a tube and sheath) was the first biological assembly reconstructed in three dimensions by electron microscopy at a resolution of ∼35 Å in 1968. A single-particle reconstruction of the T4 baseplate was able to generate a 4.1 Å resolution map for the first two rings of the tube using the overall baseplate for alignment. We have now reconstructed the T4 tail tube at a resolution of 3.4 Å, more than a 1,000-fold increase in information content for the tube from 1968. We have used legacy software (Spider) to show that we can do better than the typical 2/3 Nyquist frequency. A reasonable map can be generated with only 1.5 electrons/Å using the higher dose images for alignment, but increasing the dose results in a better map, consistent with other reports that electron dose does not represent the main limitation on resolution in cryo-electron microscopy.
External linksStructure / PubMed:28757144 / PubMed Central
MethodsEM (helical sym.)
Resolution3.4 - 3.5 Å
Structure data

EMDB-8767, PDB-5w5f:
Cryo-EM structure of the T4 tail tube
Method: EM (helical sym.) / Resolution: 3.4 Å

PDB-5w5e:
Re-refinement of the pyocin tube structure
Method: ELECTRON MICROSCOPY / Resolution: 3.5 Å

Source
  • enterobacteria phage t4 sensu lato (virus)
  • pseudomonas aeruginosa (bacteria)
KeywordsSTRUCTURAL PROTEIN / pyocin / bacteriocin / VIRAL PROTEIN / T4 tail tube / dose limit / helical reconstruction

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