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Title | Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV. |
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Journal, issue, pages | Nat Methods, Vol. 14, Issue 11, Page 1075-1078, Year 2017 |
Publish date | Oct 9, 2017 |
Authors | Mark A Herzik / Mengyu Wu / Gabriel C Lander / |
PubMed Abstract | 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 ...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 links | Nat Methods / PubMed:28991891 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.6 - 3.3 Å |
Structure data | EMDB-8741, PDB-5vy3: |
Source |
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Keywords | HYDROLASE / Proteasome / LYASE / glycolytic enzyme |