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- PDB-6rpo: bat circovirus without DNA VLP -

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Basic information

Entry
Database: PDB / ID: 6rpo
Titlebat circovirus without DNA VLP
Componentsbat circovirus capsid protein
KeywordsVIRUS LIKE PARTICLE / bat circovirus without DNA VLP
Function / homology
Function and homology information


viral capsid assembly / host cell / T=1 icosahedral viral capsid / viral penetration into host nucleus / symbiont entry into host cell / virion attachment to host cell
Similarity search - Function
Circovirus capsid protein / Circovirus capsid superfamily / Circovirus capsid protein
Similarity search - Domain/homology
Biological speciesBat circovirus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.39 Å
AuthorsForwood, J.K. / Luque, D. / Mata, C.P. / Das, S. / Raidal, S.
CitationJournal: To Be Published
Title: bat circovirus without DNA VLP
Authors: Forwood, J.K. / Luque, D. / Mata, C.P. / Das, S. / Raidal, S.
History
DepositionMay 14, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 25, 2020Provider: repository / Type: Initial release

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Structure visualization

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Assembly

Deposited unit
u: bat circovirus capsid protein


Theoretical massNumber of molelcules
Total (without water)27,7551
Polymers27,7551
Non-polymers00
Water0
1
u: bat circovirus capsid protein
x 60


Theoretical massNumber of molelcules
Total (without water)1,665,28560
Polymers1,665,28560
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1
point symmetry operation59
MethodPISA

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Components

#1: Protein bat circovirus capsid protein


Mass: 27754.744 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bat circovirus / Production host: Escherichia coli (E. coli) / References: UniProt: R4L4W6*PLUS

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Bat circovirus / Type: VIRUS / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 1.42 MDa / Experimental value: NO
Source (natural)Organism: Bat circovirus
Source (recombinant)Organism: Escherichia coli (E. coli)
Details of virusEmpty: YES / Enveloped: NO / Isolate: STRAIN / Type: VIRUS-LIKE PARTICLE
Virus shellDiameter: 200 nm / Triangulation number (T number): 1
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER/RHODIUM / Grid type: Quantifoil R2/2
VitrificationInstrument: LEICA EM CPC / Cryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER
Electron lensMode: OTHER / Nominal magnification: 47170 X / Nominal defocus max: 3500 nm / Nominal defocus min: 750 nm / Cs: 2.7 mm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 57 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 1474
Image scansMovie frames/image: 32

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Processing

SoftwareName: PHENIX / Version: dev_3311: / Classification: refinement
EM software
IDNameCategory
1Gautomatchparticle selection
2EPUimage acquisition
4RELIONCTF correction
7UCSF Chimeramodel fitting
8Cootmodel fitting
10RELIONinitial Euler assignment
11RELIONfinal Euler assignment
12RELIONclassification
13RELION3D reconstruction
14Cootmodel refinement
15PHENIXmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 124275
SymmetryPoint symmetry: I (icosahedral)
3D reconstructionResolution: 2.39 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 58147 / Num. of class averages: 1 / Symmetry type: POINT
Atomic model buildingB value: 83 / Protocol: OTHER / Space: REAL

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