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Title | Refined Cryo-EM Structure of the T4 Tail Tube: Exploring the Lowest Dose Limit. |
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Journal, issue, pages | Structure, Vol. 25, Issue 9, Page 1436-11441.e2, Year 2017 |
Publish date | Sep 5, 2017 |
Authors | Weili Zheng / Fengbin Wang / Nicholas M I Taylor / Ricardo C Guerrero-Ferreira / Petr G Leiman / Edward H Egelman / |
PubMed Abstract | 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 ...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 links | Structure / PubMed:28757144 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 3.4 - 3.5 Å |
Structure data | EMDB-8767, PDB-5w5f: PDB-5w5e: |
Source |
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Keywords | STRUCTURAL PROTEIN / pyocin / bacteriocin / VIRAL PROTEIN / T4 tail tube / dose limit / helical reconstruction |