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- EMDB-50521: Tail of emppty Haloferax tailed virus 1 -

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Basic information

Entry
Database: EMDB / ID: EMD-50521
TitleTail of emppty Haloferax tailed virus 1
Map data
Sample
  • Virus: Haloferax tailed virus 1
    • Protein or peptide: HK97 gp6-like/SPP1 gp15-like head-tail connector
    • Protein or peptide: SPP1 gp17-like tail completion protein
    • Protein or peptide: Tail tube protein
    • Protein or peptide: Baseplate to tube adapter protein gp41
  • Ligand: MAGNESIUM ION
KeywordsArcheal virus / portal / tail / VIRUS
Function / homologyHK97 gp6-like/SPP1 gp15-like head-tail connector / Tail tube protein / SPP1 gp17-like tail completion protein / Uncharacterized protein
Function and homology information
Biological speciesHaloferax tailed virus 1
Methodsingle particle reconstruction / cryo EM / Resolution: 2.96 Å
AuthorsZhang D / Daum B / Isupov MN / McLaren M
Funding supportEuropean Union, 1 items
OrganizationGrant numberCountry
European Research Council (ERC)European Union
CitationJournal: Sci Adv / Year: 2025
Title: Cryo-EM resolves the structure of the archaeal dsDNA virus HFTV1 from head to tail.
Authors: Daniel X Zhang / Michail N Isupov / Rebecca M Davies / Sabine Schwarzer / Mathew McLaren / William S Stuart / Vicki A M Gold / Hanna M Oksanen / Tessa E F Quax / Bertram Daum /
Abstract: While archaeal viruses show a stunning diversity of morphologies, many bear a notable resemblance to tailed bacterial phages. This raises fundamental questions: Do all tailed viruses share a common ...While archaeal viruses show a stunning diversity of morphologies, many bear a notable resemblance to tailed bacterial phages. This raises fundamental questions: Do all tailed viruses share a common origin and do they infect their hosts in similar ways? Answering these questions requires high-resolution structural insights, yet no complete atomic models of archaeal viruses have been available. Here, we present the near-atomic resolution structure of Haloferax tailed virus 1 (HFTV1), an archaeal virus thriving in extreme salinity. Using cryo-electron microscopy, we resolve the architecture and assembly of all structural proteins and capture conformational transitions associated with DNA ejection. Our data reveal genome spooling within the capsid and identify putative receptor-binding and catalytic sites for host recognition and infection. These findings uncover key mechanisms of archaeal virus assembly, principles of virus-host interactions, and evolutionary links connecting archaeal, bacterial, and eukaryotic viruses.
History
DepositionJun 3, 2024-
Header (metadata) releaseJun 18, 2025-
Map releaseJun 18, 2025-
UpdateOct 22, 2025-
Current statusOct 22, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_50521.png

Downloads & links

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Map

FileDownload / File: emd_50521.map.gz / Format: CCP4 / Size: 1.7 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.17 Å/pix.
x 768 pix.
= 899.328 Å		1.17 Å/pix.
x 768 pix.
= 899.328 Å		1.17 Å/pix.
x 768 pix.
= 899.328 Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.171 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0062
Minimum - Maximum-0.030950965 - 0.0727372
Average (Standard dev.)0.00012584006 (±0.0020537633)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions768768768
Spacing768768768
CellA=B=C: 899.328 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_50521_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_50521_half_map_2.map
Projections & Slices
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Sample components

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Entire : Haloferax tailed virus 1

EntireName: Haloferax tailed virus 1
Components
  • Virus: Haloferax tailed virus 1
    • Protein or peptide: HK97 gp6-like/SPP1 gp15-like head-tail connector
    • Protein or peptide: SPP1 gp17-like tail completion protein
    • Protein or peptide: Tail tube protein
    • Protein or peptide: Baseplate to tube adapter protein gp41
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Haloferax tailed virus 1

SupramoleculeName: Haloferax tailed virus 1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 / NCBI-ID: 2507575 / Sci species name: Haloferax tailed virus 1 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes
Host (natural)Organism: Haloferax gibbonsii (archaea)

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Macromolecule #1: HK97 gp6-like/SPP1 gp15-like head-tail connector

MacromoleculeName: HK97 gp6-like/SPP1 gp15-like head-tail connector / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Haloferax tailed virus 1
Molecular weightTheoretical: 15.585868 KDa
SequenceString:
MPDPSIDEVS KSDWDALTTQ EQDDIISQVE NLSSTGWVNT SRERKAEAIR SAIAERDTLY SGNMSRLPTL DGDAEYFTLY LSAHKIQLF EGGEAQSESG EGGSVSYSTG GGGEKDLQKT RYGRMALEYV WEDNSIAALR TY

UniProtKB: HK97 gp6-like/SPP1 gp15-like head-tail connector

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Macromolecule #2: SPP1 gp17-like tail completion protein

MacromoleculeName: SPP1 gp17-like tail completion protein / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Haloferax tailed virus 1
Molecular weightTheoretical: 17.458789 KDa
SequenceString:
MATTSASHHV QAIIDLLEAA PDADWTPTQT PTVKRYWDDA QSERGPGADM PAILYVWSPT TSSLDRFSMD GDVFDQNDSI EVQAWSFDE TEVEQLQGDI VQILSEYLDD NEVQTPYSDV APTGTNDFRE QTPARTTGHY IMSVEVETRG LSETAKNA

UniProtKB: SPP1 gp17-like tail completion protein

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Macromolecule #3: Tail tube protein

MacromoleculeName: Tail tube protein / type: protein_or_peptide / ID: 3 / Number of copies: 66 / Enantiomer: LEVO
Source (natural)Organism: Haloferax tailed virus 1
Molecular weightTheoretical: 17.177463 KDa
SequenceString:
MATSPEGIWS NSGALTFEDP ADDSEILFAG VRDVTITPAY EHAELYTIDS TFRDEVKRYE HNVNVEITYA KFSLEFAQEW LGGPGATAT ASQDDSDPMK FNLENVTPSA SGGFERTTAV ENVVFPELPL DSATYGEYEE YSLTGSGRSV TNLADTSGV

UniProtKB: Tail tube protein

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Macromolecule #4: Baseplate to tube adapter protein gp41

MacromoleculeName: Baseplate to tube adapter protein gp41 / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Haloferax tailed virus 1
Molecular weightTheoretical: 30.425914 KDa
SequenceString: MVDATLSRGG TSVDIPLVEE GGEILLSSTF GKPEVNVRKS GGSLNPRVID SWSGLQTFQL VGKLYDYSTS HQLADLVKTA STTPLELQI PQDAYPDTVT VAPAAGQASA LTLEYPAGRK DLVDVSLSLT RVDPNSVRGV GDQQATTPTT TGTGPVEVTA G GTTVQLPS ...String:
MVDATLSRGG TSVDIPLVEE GGEILLSSTF GKPEVNVRKS GGSLNPRVID SWSGLQTFQL VGKLYDYSTS HQLADLVKTA STTPLELQI PQDAYPDTVT VAPAAGQASA LTLEYPAGRK DLVDVSLSLT RVDPNSVRGV GDQQATTPTT TGTGPVEVTA G GTTVQLPS SGLSVERTVG RPNDAVRRVP RQADPRYEVK AKVTNDVFTF SFETLDNIPA TLNALTDNVF REQLGRDGVT LD FNGLLGL GSVKAIPVGS SPFRQVHQAG RGWVTVPTLE FRRIYSNE

UniProtKB: Uncharacterized protein

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Macromolecule #5: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 5 / Number of copies: 12 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recording#0 - Image recording ID: 1 / #0 - Film or detector model: TFS FALCON 4i (4k x 4k) / #0 - Average electron dose: 50.0 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K3 (6k x 4k) / #1 - Average electron dose: 54.6 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Image recording ID2
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.96 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 6580
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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