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- PDB-11lx: Bacteriophage Goslar Baseplate -

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Basic information

Entry
Database: PDB / ID: 11lx
TitleBacteriophage Goslar Baseplate
Components
  • (Inner Baseplate Protein ...) x 4
  • (Virion structural ...) x 2
  • Baseplate wedge protein
  • SH3 fold domain-containing protein
  • Tail Tube Initiator Protein gp62
  • Tail Tube of Bacteriophage Goslar
  • Tail sheath protein gp29 gp29PR domain-containing protein
  • Tail tube initiator complex protein gp203
KeywordsVIRAL PROTEIN / Collar / WAC / Whiskers
Function / homology
Function and homology information


SH3 fold domain associated with phage DNA polymerases / : / : / SH3 fold domain associated with phage DNA polymerases / Family of unknown function (DUF7194) / Putative phage tail tube protein / : / Family of unknown function (DUF7208) / : / Phage tail tube protein ...SH3 fold domain associated with phage DNA polymerases / : / : / SH3 fold domain associated with phage DNA polymerases / Family of unknown function (DUF7194) / Putative phage tail tube protein / : / Family of unknown function (DUF7208) / : / Phage tail tube protein / : / Bacteriophage phiKZ, gp29PR
Similarity search - Domain/homology
Virion structural protein / Uncharacterized protein / Uncharacterized protein / SH3 fold domain-containing protein / Uncharacterized protein / Uncharacterized protein / Baseplate wedge protein / Tail sheath protein gp29 gp29PR domain-containing protein / Virion structural protein / Uncharacterized protein ...Virion structural protein / Uncharacterized protein / Uncharacterized protein / SH3 fold domain-containing protein / Uncharacterized protein / Uncharacterized protein / Baseplate wedge protein / Tail sheath protein gp29 gp29PR domain-containing protein / Virion structural protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein
Similarity search - Component
Biological speciesGoslarvirus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.88 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: Bacteriophage Goslar Baseplate
Authors: Basu, D.
History
DepositionMar 3, 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

Downloads & links

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Assembly

Deposited unit
AJ: Tail Tube Initiator Protein gp62
AO: Tail Tube of Bacteriophage Goslar
Aa: Virion structural protein
Ab: Virion structural protein
Ah: Tail sheath protein gp29 gp29PR domain-containing protein
An: Tail sheath protein gp29 gp29PR domain-containing protein
Aq: Baseplate wedge protein
Az: Tail sheath protein gp29 gp29PR domain-containing protein
Bh: Virion structural protein
CJ: Inner baseplate protein gp202
H: Tail tube initiator complex protein gp203
I: Inner Baseplate Protein gp172
M: Baseplate wedge protein
V: SH3 fold domain-containing protein
W: SH3 fold domain-containing protein
X: Inner Baseplate Protein gp180
n: Inner Baseplate Protein gp187
o: Inner Baseplate Protein gp187
s: SH3 fold domain-containing protein
t: SH3 fold domain-containing protein


Theoretical massNumber of molelcules
Total (without water)945,57120
Polymers945,57120
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

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Protein , 6 types, 12 molecules AJAOAhAnAzAqMHVWst

#1: Protein Tail Tube Initiator Protein gp62


Mass: 46241.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GMY4
#2: Protein Tail Tube of Bacteriophage Goslar


Mass: 32990.105 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GE68
#4: Protein Tail sheath protein gp29 gp29PR domain-containing protein


Mass: 76777.891 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GKT6
#5: Protein Baseplate wedge protein


Mass: 112287.836 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GHK3
#8: Protein Tail tube initiator complex protein gp203


Mass: 77510.961 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GEN9
#10: Protein
SH3 fold domain-containing protein


Mass: 15191.130 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GEK6

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Virion structural ... , 2 types, 3 molecules AaAbBh

#3: Protein Virion structural protein


Mass: 32893.969 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GMW3
#6: Protein Virion structural protein


Mass: 93934.773 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GE11

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Inner Baseplate Protein ... , 4 types, 5 molecules CJIXno

#7: Protein Inner baseplate protein gp202


Mass: 38813.621 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GNB0
#9: Protein Inner Baseplate Protein gp172


Mass: 13531.216 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GN61
#11: Protein Inner Baseplate Protein gp180


Mass: 15230.221 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GH49
#12: Protein Inner Baseplate Protein gp187


Mass: 22928.111 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Goslarvirus / References: UniProt: A0A482GE98

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Details

Has protein modificationY

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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
3D reconstructionResolution: 3.88 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 31110 / Symmetry type: POINT
Atomic model buildingSource name: AlphaFold / Type: in silico model

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