4UDV
Cryo-EM structure of TMV at 3.35 A resolution
Summary for 4UDV
Entry DOI | 10.2210/pdb4udv/pdb |
EMDB information | 2842 |
Descriptor | CAPSID PROTEIN, 5'-D(*GP*AP*AP)-3' (2 entities in total) |
Functional Keywords | viral protein, direct electron detectors, single particle helical reconstruction, high resolution |
Biological source | TOBACCO MOSAIC VIRUS More |
Total number of polymer chains | 2 |
Total formula weight | 18464.09 |
Authors | Fromm, S.A.,Bharat, T.A.M.,Jakobi, A.J.,Hagen, W.J.H.,Sachse, C. (deposition date: 2014-12-11, release date: 2014-12-31, Last modification date: 2024-05-08) |
Primary citation | Fromm, S.A.,Bharat, T.A.M.,Jakobi, A.J.,Hagen, W.J.H.,Sachse, C. Seeing Tobacco Mosaic Virus Through Direct Electron Detectors. J.Struct.Biol., 189:87-, 2015 Cited by PubMed Abstract: With the introduction of direct electron detectors (DED) to the field of electron cryo-microscopy, a wave of atomic-resolution structures has become available. As the new detectors still require comparative characterization, we have used tobacco mosaic virus (TMV) as a test specimen to study the quality of 3D image reconstructions from data recorded on the two direct electron detector cameras, K2 Summit and Falcon II. Using DED movie frames, we explored related image-processing aspects and compared the performance of micrograph-based and segment-based motion correction approaches. In addition, we investigated the effect of dose deposition on the atomic-resolution structure of TMV and show that radiation damage affects negative carboxyl chains first in a side-chain specific manner. Finally, using 450,000 asymmetric units and limiting the effects of radiation damage, we determined a high-resolution cryo-EM map at 3.35Å resolution. Here, we provide a comparative case study of highly ordered TMV recorded on different direct electron detectors to establish recording and processing conditions that enable structure determination up to 3.2Å in resolution using cryo-EM. PubMed: 25528571DOI: 10.1016/J.JSB.2014.12.002 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.35 Å) |
Structure validation
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