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Open data
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Basic information
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| Title | Tail of full Haloferax tailed virus 1 | |||||||||
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Keywords | Archaeal virus / portal / tail / baseplate / tape measure protein / VIRUS | |||||||||
| Function / homology | Portal protein / HK97 gp6-like/SPP1 gp15-like head-tail connector / Baseplate hub / Tail tube protein / SPP1 gp17-like tail completion protein / Phate tail tape measure protein / Uncharacterized protein Function and homology information | |||||||||
| Biological species | Haloferax tailed virus 1 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.44 Å | |||||||||
Authors | Zhang D / Daum B / Isupov MN / McLaren M | |||||||||
| Funding support | European Union, 1 items
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Citation | Journal: Sci Adv / Year: 2025Title: 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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_51866.map.gz | 1.6 GB | EMDB map data format | |
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| Header (meta data) | emd-51866-v30.xml emd-51866.xml | 25.2 KB 25.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51866_fsc.xml | 26.8 KB | Display | FSC data file |
| Images | emd_51866.png | 44.7 KB | ||
| Filedesc metadata | emd-51866.cif.gz | 7.7 KB | ||
| Others | emd_51866_half_map_1.map.gz emd_51866_half_map_2.map.gz | 1.4 GB 1.4 GB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51866 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51866 | HTTPS FTP |
-Validation report
| Summary document | emd_51866_validation.pdf.gz | 840.3 KB | Display | EMDB validaton report |
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| Full document | emd_51866_full_validation.pdf.gz | 839.8 KB | Display | |
| Data in XML | emd_51866_validation.xml.gz | 34 KB | Display | |
| Data in CIF | emd_51866_validation.cif.gz | 46.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51866 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51866 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9h4pMC ![]() 8qpgC ![]() 8qpqC ![]() 8qqnC ![]() 8qsiC ![]() 8qsyC ![]() 9fkbC ![]() 9gs0C ![]() 9h5bC ![]() 9h7vC 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_51866.map.gz / Format: CCP4 / Size: 1.7 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.171 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_51866_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_51866_half_map_2.map | ||||||||||||
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Sample components
-Entire : Haloferax tailed virus 1
| Entire | Name: Haloferax tailed virus 1 |
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| Components |
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-Supramolecule #1: Haloferax tailed virus 1
| Supramolecule | Name: Haloferax tailed virus 1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#7 / NCBI-ID: 2507575 / Sci species name: Haloferax tailed virus 1 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes |
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| Host (natural) | Organism: Haloferax gibbonsii (archaea) |
-Macromolecule #1: Baseplate hub
| Macromolecule | Name: Baseplate hub / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 102.541312 KDa |
| Sequence | String: MPQLGDSKLG ESQLGSPGTL KQGVEWTVVV DGEEQNNVWD VQVVDTANPF GDYAVFKMDD RGGQAFEAYP RGTRVEAYVS EGTEPLDNR FTGYVVERRE NEQQGADVLE VEAYSFDQFL RRNTVTNDQT GNTISQALAD IIQTDTPVRF NAANITVGDD Q ELTRSYQG ...String: MPQLGDSKLG ESQLGSPGTL KQGVEWTVVV DGEEQNNVWD VQVVDTANPF GDYAVFKMDD RGGQAFEAYP RGTRVEAYVS EGTEPLDNR FTGYVVERRE NEQQGADVLE VEAYSFDQFL RRNTVTNDQT GNTISQALAD IIQTDTPVRF NAANITVGDD Q ELTRSYQG DPVENALRDF AFKSTNEDFG VGDDLEFFFQ PRETVHIDRG VDNTQWFRYD IPELGKEAIN EVEVWFDDGE ES VIVDDGT DKLDLQDSLG LPSPGTQRKE LQRPLVTDIS DAEDIGRKYL AFRNSTLSGT VTTYGLYDAE PGDTIDITID PRG IDEEFV IAAIEYRWGV DETILTVVEK RGDVDDILSE LSESVQRIEM QGANRDAPKN RITTTNAAAI VSVDVDAGGT SADA DRFVN DGRNAVRDAW TGAGNPDIAN IVVGDDNSGL SRTNTTLGNQ TDSVSVTESL PSAKVVEYSA TLTQSGVEEI GLETS TGTL LTRATFETPV DLSSDTVTVT LTVSNDDSVS RGVMTNDGQT AVRDVLADNS PTLPTDYGYG DDSTAVAETD TTLGNE LAN TSLEEILIQS ASSVSAWNTI LGTLASTYPL VVSSSGIRPA QTAWTTESDN LAQSGTALVT VGDYSNGEAE GLDSPGD TL ELSFTPEHDI PGEEFALWCR IETDLGGTDP GPEITVTLDI DGDTYSWVPI GTNTALGLNW YDLANNTFGG SSTYPDTD I PEGSTVTLSI EATSSSVSGQ GHAVDVMAPL DALTRVTGGS DATSAYTFDN NNGGSGGYLD GPELYPDQLI LSLETATTR RNVSEARFTL TANDTSGNFY VELANDGSTF NRVNNATSGS VTFASPDTNV DTNISLNRYG SRSTATPQTG FNAQEIDNWE LYADIDAVL PDDIGVTLSR AIIPPNTSGI VGQTVREAGL KSGSTLLTRH ILAEFLLDTD QRLASSESTR FTSDN UniProtKB: Baseplate hub |
-Macromolecule #2: Phate tail tape measure protein
| Macromolecule | Name: Phate tail tape measure protein / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 36.043656 KDa |
| Sequence | String: MVAIRSEGVS ETQQNLEGVE NAMEDTADSA GDSAAELETF SKRFKGAMGA AVSALAIGTA GLLSQVPVVG EAMGGLGAII DALTMKIDE DARPAVGSFT DDLYEVAEAT YEADSSLEAF QTALDGVNTA IDDVAVSTLQ TEIEELTGIT IPKNWLDFGW D IMTLDARQ ...String: MVAIRSEGVS ETQQNLEGVE NAMEDTADSA GDSAAELETF SKRFKGAMGA AVSALAIGTA GLLSQVPVVG EAMGGLGAII DALTMKIDE DARPAVGSFT DDLYEVAEAT YEADSSLEAF QTALDGVNTA IDDVAVSTLQ TEIEELTGIT IPKNWLDFGW D IMTLDARQ TMDNIETIIN EFPEDFGTML KSIDPRAKKG WDILTKSADM FINDLTSRID SGVNDVRGFF TGLASDLNEW GG NVASDAR EWGTNLIDKF TGGIRSKISG LRNWLSELRN IGAEVGIDVP TIGGGGDGGG GGGNSSRQPF AGGFFGGGNA TID GRQISE STGRYRSDPS RRRGI UniProtKB: Phate tail tape measure protein |
-Macromolecule #3: Baseplate to tube adapter protein gp41
| Macromolecule | Name: Baseplate to tube adapter protein gp41 / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 30.425914 KDa |
| Sequence | String: 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 |
-Macromolecule #4: Tail tube protein
| Macromolecule | Name: Tail tube protein / type: protein_or_peptide / ID: 4 / Number of copies: 66 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 17.177463 KDa |
| Sequence | String: MATSPEGIWS NSGALTFEDP ADDSEILFAG VRDVTITPAY EHAELYTIDS TFRDEVKRYE HNVNVEITYA KFSLEFAQEW LGGPGATAT ASQDDSDPMK FNLENVTPSA SGGFERTTAV ENVVFPELPL DSATYGEYEE YSLTGSGRSV TNLADTSGV UniProtKB: Tail tube protein |
-Macromolecule #5: SPP1 gp17-like tail completion protein
| Macromolecule | Name: SPP1 gp17-like tail completion protein / type: protein_or_peptide / ID: 5 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 17.458789 KDa |
| Sequence | String: MATTSASHHV QAIIDLLEAA PDADWTPTQT PTVKRYWDDA QSERGPGADM PAILYVWSPT TSSLDRFSMD GDVFDQNDSI EVQAWSFDE TEVEQLQGDI VQILSEYLDD NEVQTPYSDV APTGTNDFRE QTPARTTGHY IMSVEVETRG LSETAKNA UniProtKB: SPP1 gp17-like tail completion protein |
-Macromolecule #6: HK97 gp6-like/SPP1 gp15-like head-tail connector
| Macromolecule | Name: HK97 gp6-like/SPP1 gp15-like head-tail connector / type: protein_or_peptide / ID: 6 / Number of copies: 12 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 15.585868 KDa |
| Sequence | String: 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 |
-Macromolecule #7: Portal protein
| Macromolecule | Name: Portal protein / type: protein_or_peptide / ID: 7 / Number of copies: 12 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 75.680906 KDa |
| Sequence | String: MPKYNLRIGN RRVPIASTDT PLSEAIGKRL ASSTPQTNVD SMGGGHSYQF NGQDLTFEDL RDIKDVRDSG GQVAQLMDYK ALLNFGEGC EIHVEGDDET KQLVDGEPMT LSEWLEDAFP HLDLLVLDLG GDALWYPYAV GEIQETITGE FKEALPAEPW T LMPESDAQ ...String: MPKYNLRIGN RRVPIASTDT PLSEAIGKRL ASSTPQTNVD SMGGGHSYQF NGQDLTFEDL RDIKDVRDSG GQVAQLMDYK ALLNFGEGC EIHVEGDDET KQLVDGEPMT LSEWLEDAFP HLDLLVLDLG GDALWYPYAV GEIQETITGE FKEALPAEPW T LMPESDAQ GKVQAWHQRT KTHGGYQTQT LPADDLW(HIP)IV INKASARDEV GISEVLRNKD EIQAFKQNEA AINQAIEL H GFPQR(HIP)VKVG KEDGAPVRDN DLRRVRTIFD PRTTDANTAY FTGQDVDVET LEA(HIP)NFDYSA IHEMDMRNLT T ALGLPLEA GNVGADGLGS GKPAELRFAL LKLAIKANQR SFSVQFVERV MRPVVRDYSP FDHEADIRLE INDPLEDIGE VA DLIQQVG DYMTNEQVAE KLDLPAPEDD EVADSYRSPA DMEKDEAGVQ DEPFGGMFAG RDMGNRCLGE GITDDELQHA PEW DRPLLE MYQGVTNPES DTSRTLVSFS SSGTPEFVLE RIRESIMDGA LFSEFDNIPS SRLMELRQTF ADELGTDNFT LDSI TDALM DFEADLTRDA AERIARTESS AVLNHAREIS YEERGEGNEL FYWTGADLGD SRQTEACAWL IRQTNPFSGG TPVPM NELR DMVDEAPSHD DSMDNNLARP DSWVVHPNER SSFVKAPPNW EQL UniProtKB: Portal protein |
-Macromolecule #8: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 8 / Number of copies: 15 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-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 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| 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 beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination 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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About Yorodumi




Haloferax tailed virus 1
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Haloferax gibbonsii (archaea)
Processing
FIELD EMISSION GUN

