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- EMDB-16857: Extended cowpea chlorotic mottle virus at pH 7.6 in plunge-frozen... -

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Basic information

Entry
Database: EMDB / ID: EMD-16857
TitleExtended cowpea chlorotic mottle virus at pH 7.6 in plunge-frozen vitrified ice
Map data
Sample
  • Virus: Cowpea chlorotic mottle virus
KeywordsIcosahedral / extended / virus
Biological speciesCowpea chlorotic mottle virus
Methodsingle particle reconstruction / cryo EM / Resolution: 4.1 Å
AuthorsHarder OF / Barrass SV / Drabbels M / Lorenz UJ
Funding support Switzerland, European Union, 2 items
OrganizationGrant numberCountry
Swiss National Science FoundationPP00P2_163681 Switzerland
European Research Council (ERC)759145European Union
CitationJournal: Nat Commun / Year: 2023
Title: Fast viral dynamics revealed by microsecond time-resolved cryo-EM.
Authors: Oliver F Harder / Sarah V Barrass / Marcel Drabbels / Ulrich J Lorenz /
Abstract: Observing proteins as they perform their tasks has largely remained elusive, which has left our understanding of protein function fundamentally incomplete. To enable such observations, we have ...Observing proteins as they perform their tasks has largely remained elusive, which has left our understanding of protein function fundamentally incomplete. To enable such observations, we have recently proposed a technique that improves the time resolution of cryo-electron microscopy (cryo-EM) to microseconds. Here, we demonstrate that microsecond time-resolved cryo-EM enables observations of fast protein dynamics. We use our approach to elucidate the mechanics of the capsid of cowpea chlorotic mottle virus (CCMV), whose large-amplitude motions play a crucial role in the viral life cycle. We observe that a pH jump causes the extended configuration of the capsid to contract on the microsecond timescale. While this is a concerted process, the motions of the capsid proteins involve different timescales, leading to a curved reaction path. It is difficult to conceive how such a detailed picture of the dynamics could have been obtained with any other method, which highlights the potential of our technique. Crucially, our experiments pave the way for microsecond time-resolved cryo-EM to be applied to a broad range of protein dynamics that previously could not have been observed. This promises to fundamentally advance our understanding of protein function.
History
DepositionMar 15, 2023-
Header (metadata) releaseSep 27, 2023-
Map releaseSep 27, 2023-
UpdateOct 18, 2023-
Current statusOct 18, 2023Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_16857.map.gz / Format: CCP4 / Size: 1.7 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.726 Å
Density
Contour LevelBy AUTHOR: 0.0309
Minimum - Maximum-0.05760501 - 0.13866904
Average (Standard dev.)-0.0007067977 (±0.0076762703)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions768768768
Spacing768768768
CellA=B=C: 557.568 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_16857_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_16857_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Cowpea chlorotic mottle virus

EntireName: Cowpea chlorotic mottle virus
Components
  • Virus: Cowpea chlorotic mottle virus

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Supramolecule #1: Cowpea chlorotic mottle virus

SupramoleculeName: Cowpea chlorotic mottle virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1 / NCBI-ID: 12303 / Sci species name: Cowpea chlorotic mottle virus / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No
Virus shellShell ID: 1 / T number (triangulation number): 3

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.6
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 0.9 µm / Nominal defocus min: 0.3 µm
Specialist opticsEnergy filter - Name: TFS Selectris X / Energy filter - Slit width: 10 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Alignment procedureComa free - Residual tilt: 150.0 mrad
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 0.726 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 203268
Startup modelType of model: INSILICO MODEL
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.0.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionApplied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 79910

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