8VG6
Structure of Tulane virus
Summary for 8VG6
| Entry DOI | 10.2210/pdb8vg6/pdb |
| EMDB information | 8252 |
| Descriptor | Capsid protein (1 entity in total) |
| Functional Keywords | tualne virus, calicivirus, norovirus, virus |
| Biological source | Tulane virus |
| Total number of polymer chains | 3 |
| Total formula weight | 173670.17 |
| Authors | |
| Primary citation | Yu, G.,Li, K.,Huang, P.,Jiang, X.,Jiang, W. Antibody-Based Affinity Cryoelectron Microscopy at 2.6- angstrom Resolution. Structure, 24:1984-1990, 2016 Cited by PubMed Abstract: 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. PubMed: 27806259DOI: 10.1016/j.str.2016.09.008 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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