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- PDB-11ec: Tail Tube of Bacteriophage Goslar -

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Basic information

Entry
Database: PDB / ID: 11ec
TitleTail Tube of Bacteriophage Goslar
ComponentsTail Tube of Bacteriophage Goslar
KeywordsVIRAL PROTEIN / Tail tube / Phage
Function / homology: / Phage tail tube protein / Uncharacterized protein
Function and homology information
Biological speciesGoslarvirus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.22 Å
AuthorsBasu, D. / Gu, Y. / Corbett, K.D.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI)Emerging Pathogens Initiative United States
CitationJournal: To Be Published
Title: Tail Tube of Bacteriophage Goslar
Authors: Basu, D.
History
DepositionFeb 18, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 19, 2026Provider: repository / Type: Initial release
Revision 1.0Aug 19, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
AG: Tail Tube of Bacteriophage Goslar
AH: Tail Tube of Bacteriophage Goslar
AI: Tail Tube of Bacteriophage Goslar
AJ: Tail Tube of Bacteriophage Goslar
AK: Tail Tube of Bacteriophage Goslar
AL: Tail Tube of Bacteriophage Goslar
AM: Tail Tube of Bacteriophage Goslar
AN: Tail Tube of Bacteriophage Goslar
AO: Tail Tube of Bacteriophage Goslar
AP: Tail Tube of Bacteriophage Goslar
AQ: Tail Tube of Bacteriophage Goslar
AR: Tail Tube of Bacteriophage Goslar


Theoretical massNumber of molelcules
Total (without water)395,88112
Polymers395,88112
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Tail Tube of Bacteriophage Goslar


Mass: 32990.105 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GE68
Has protein modificationN

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: Goslarvirus / Type: VIRUS / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Goslarvirus
Details of virusEmpty: NO / Enveloped: NO / Isolate: STRAIN / Type: VIRION
Natural hostOrganism: Escherichia coli
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid type: Quantifoil
VitrificationInstrument: FEI VITROBOT MARK II / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 277 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2EPUimage acquisition
7UCSF ChimeraXmodel fitting
9PHENIXmodel refinement
13cryoSPARC4.7.13D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C6 (6 fold cyclic)
3D reconstructionResolution: 3.22 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1143360 / Symmetry type: POINT
Atomic model buildingSource name: AlphaFold / Type: in silico model

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