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Open data
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Basic information
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| Title | Icosahedral Capsid assembly of phage Oekolampad (Bas18) | |||||||||
Map data | Icosahedral Capsid assembly of phage Oekolampad (Bas18) | |||||||||
Sample |
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Keywords | Bacteriophage / Cryo-EM SPA / VIRUS | |||||||||
| Function / homology | Major capsid protein 13-like / Major capsid protein 13-like / Uncharacterized protein / Major capsid protein Function and homology information | |||||||||
| Biological species | ![]() Escherichia phage Oekolampad (virus) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Rosheny K / Harry M / Mike S / Mihnea B | |||||||||
| Funding support | 1 items
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Citation | Journal: J Mol Biol / Year: 2026Title: A classic fold with a twist: Structural architecture of Dhillonvirus phage Bas18. Authors: Rosheny Kumaran / Harry McFarlane / Caitlin J Ewenson / Klemens McJarrow-Keller / Alice-Roza Eruera / Mike Strauss / Mihnea Bostina / ![]() Abstract: Although over 15,000 unique phage genomes have been sequenced, many isolates remain uncharacterised and accessible only within individual laboratories. The BASEL (BActeriophage SElection for your ...Although over 15,000 unique phage genomes have been sequenced, many isolates remain uncharacterised and accessible only within individual laboratories. The BASEL (BActeriophage SElection for your Laboratory) collection comprises 106 newly isolated and characterised virulent bacteriophages that infect the laboratory strain Escherichia coli K-12 and provide an open resource for phage biology. Here, we used cryo-electron microscopy (cryo-EM) to determine the structure of Bas18, a Dhillonvirus siphophage from the BASEL collection. Bas18 assembles an icosahedral capsid with T=7(d) triangulation. The asymmetric unit contains seven copies of the major capsid protein (MCP; gp09) and one dimeric decoration protein (gp64) bound at the centre of each hexamer. The MCP adopts the canonical HK97 fold but features a distinct insertion between the A and P domains, which we designate as G and E loop. The neck assembly consists of the portal, adaptor, stopper and terminator. The helical tail is built from hexameric rings of the tail tube protein, and the tail tip consists of the distal tail protein, hub and central fibre. Despite low sequence similarity, the overall architecture of the neck, tail, and tail tip closely resembles that of bacteriophage T1. In contrast, structural protein sequences are highly conserved (85-99% sequence similarity) across Dhillonviruses indicating a conserved virion architecture within this genus. These results expand the structural knowledge of the BASEL collection and provide a detailed architectural framework for Dhillonvirus phages, contributing to a broader understanding of siphophage structural diversity. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_74964.map.gz | 7.2 GB | EMDB map data format | |
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| Header (meta data) | emd-74964-v30.xml emd-74964.xml | 17.7 KB 17.7 KB | Display Display | EMDB header |
| Images | emd_74964.png | 172 KB | ||
| Filedesc metadata | emd-74964.cif.gz | 5.7 KB | ||
| Others | emd_74964_half_map_1.map.gz emd_74964_half_map_2.map.gz | 6.4 GB 6.4 GB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-74964 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-74964 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9zysMC ![]() 10ecC ![]() 10ljC ![]() 10xwC ![]() 23gdC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_74964.map.gz / Format: CCP4 / Size: 7.8 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Icosahedral Capsid assembly of phage Oekolampad (Bas18) | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.855 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Half Map B
| File | emd_74964_half_map_1.map | ||||||||||||
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| Annotation | Half Map B | ||||||||||||
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| Density Histograms |
-Half map: Half Map A
| File | emd_74964_half_map_2.map | ||||||||||||
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| Annotation | Half Map A | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Escherichia phage Oekolampad
| Entire | Name: Escherichia phage Oekolampad (virus) |
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| Components |
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-Supramolecule #1: Escherichia phage Oekolampad
| Supramolecule | Name: Escherichia phage Oekolampad / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all Details: Escherichia phage Oekolampad was propagated in Escherichia coli K-12 NCBI-ID: 2851982 / Sci species name: Escherichia phage Oekolampad / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No |
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| Host (natural) | Organism: ![]() |
| Virus shell | Shell ID: 1 / T number (triangulation number): 7 |
-Macromolecule #1: Major capsid protein gp09
| Macromolecule | Name: Major capsid protein gp09 / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 38.479785 KDa |
| Sequence | String: MSLTVFQRKL VTAVTQMIPD NLNVFNAAAN GAVVLGTGEV LKDVIEKMSV GLIANLVTDR NAYAPVGTPA TAKVLARMLT NSVNLSAKV GPVAITKAMM AKIETNVNSV AAEIAAQATQ AIMLHYLKAG IGASKAAIES NAAAKYTQPA RVDGVGGRTF P TLADFPLA ...String: MSLTVFQRKL VTAVTQMIPD NLNVFNAAAN GAVVLGTGEV LKDVIEKMSV GLIANLVTDR NAYAPVGTPA TAKVLARMLT NSVNLSAKV GPVAITKAMM AKIETNVNSV AAEIAAQATQ AIMLHYLKAG IGASKAAIES NAAAKYTQPA RVDGVGGRTF P TLADFPLA ASKFGDQASL IKSWFMDGVT WANFIAYQAL PSAEQVFAIG DLQVMGDGLG RRFIISDAAA DAMGAGNMLG LV PGAVAVT TNGLDMLAQE KGGNENIERW WQGEFDFNVA VKGYRLKASA RTPIEGVRSF KLSDITTKDN WELDQGQVDN APA TVQDVG AVGDGDTKGR RKTQAAQEVP TRHIKETAGV LVTLTATTAS UniProtKB: Major capsid protein |
-Macromolecule #2: Decoration protein gp64
| Macromolecule | Name: Decoration protein gp64 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 5.590318 KDa |
| Sequence | String: MLKSILDHNA DALAALAKTE DPGARAIIAD TISHAGIFDA KLPSPPPPEE PGPAA UniProtKB: Uncharacterized protein |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.2 |
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 294.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 30.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.75 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Protocol: FLEXIBLE FIT |
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| Output model | ![]() PDB-9zys: |
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Escherichia phage Oekolampad (virus)
Keywords
Authors
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FIELD EMISSION GUN
