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4UDV

Cryo-EM structure of TMV at 3.35 A resolution

Summary for 4UDV
Entry DOI10.2210/pdb4udv/pdb
EMDB information2842
DescriptorCAPSID PROTEIN, 5'-D(*GP*AP*AP)-3' (2 entities in total)
Functional Keywordsviral protein, direct electron detectors, single particle helical reconstruction, high resolution
Biological sourceTOBACCO MOSAIC VIRUS
More
Total number of polymer chains2
Total formula weight18464.09
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 citationFromm, 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: 25528571
DOI: 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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数据于2024-10-30公开中

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