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TitleAchieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV.
Journal, issue, pagesNat Methods, Vol. 14, Issue 11, Page 1075-1078, Year 2017
Publish dateOct 9, 2017
AuthorsMark A Herzik / Mengyu Wu / Gabriel C Lander /
PubMed AbstractNearly all single-particle cryo-EM structures resolved to better than 4-Å resolution have been determined using 300-keV transmission electron microscopes (TEMs). We demonstrate that it is possible ...Nearly all single-particle cryo-EM structures resolved to better than 4-Å resolution have been determined using 300-keV transmission electron microscopes (TEMs). We demonstrate that it is possible to obtain reconstructions of macromolecular complexes of different sizes to better than 3-Å resolution using a 200-keV TEM. These structures are of sufficient quality to unambiguously assign amino acid rotameric conformations and identify ordered water molecules.
External linksNat Methods / PubMed:28991891 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.3 Å
Structure data

EMDB-8741, PDB-5vy3:
Thermoplasma acidophilum 20S Proteasome using 200keV with stage position
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-8742, PDB-5vy4:
Thermoplasma acidophilum 20S Proteasome using 200keV with image shift
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-8743, PDB-5vy5:
Rabbit muscle aldolase using 200keV
Method: EM (single particle) / Resolution: 2.6 Å

Source
  • thermoplasma acidophilum (acidophilic)
  • oryctolagus cuniculus (rabbit)
KeywordsHYDROLASE / Proteasome / LYASE / glycolytic enzyme

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