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TitleAntibody-Based Affinity Cryoelectron Microscopy at 2.6-Å Resolution.
Journal, issue, pagesStructure, Vol. 24, Issue 11, Page 1984-1990, Year 2016
Publish dateNov 1, 2016
AuthorsGuimei Yu / Kunpeng Li / Pengwei Huang / Xi Jiang / Wen Jiang /
PubMed AbstractThe affinity cryoelectron microscopy (cryo-EM) approach has been explored in recent years to simplify and/or improve the sample preparation for cryo-EM, which can bring previously challenging ...The affinity cryoelectron microscopy (cryo-EM) approach has been explored in recent years to simplify and/or improve the sample preparation for cryo-EM, which can bring previously challenging specimens such as those of low abundance and/or unpurified ones within reach of the cryo-EM technique. Despite the demonstrated successes for solving structures to low to intermediate resolutions, the lack of near-atomic structures using this approach has led to a common perception of affinity cryo-EM as a niche technique incapable of reaching high resolutions. Here, we report a ∼2.6-Å structure solved using the antibody-based affinity grid approach with low-concentration Tulane virus purified from a low-yield cell-culture system that has been challenging to standard cryo-EM grid preparation. Quantitative analyses of the structure indicate data and reconstruction quality comparable with the conventional grid preparation method using samples at high concentration.
External linksStructure / PubMed:27806259 / PubMed Central
MethodsEM (single particle)
Resolution2.6 Å
Structure data

EMDB-8252:
2.6A 3D reconstruction of Tulane virus
Method: EM (single particle) / Resolution: 2.6 Å

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