Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM resolves the structure of the archaeal dsDNA virus HFTV1 from head to tail.
Journal, issue, pages	Sci Adv, Vol. 11, Issue 40, Page eadx1178, Year 2025
Publish date	Oct 3, 2025
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 /
PubMed 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.
External links	Sci Adv / PubMed:41042861 / PubMed Central
Methods	EM (single particle)
Resolution	2.342 - 3.6 Å
Structure data	18550 8qpg EMDB-18550, PDB-8qpg: Turret of Haloferax tailed virus 1 Method: EM (single particle) / Resolution: 2.36 Å 18559 8qpq EMDB-18559, PDB-8qpq: C1 turret to capsid interface of full Haloferax tailed virus 1 adjacent to the portal-capsid interface. Method: EM (single particle) / Resolution: 2.7 Å 18599 8qqn EMDB-18599, PDB-8qqn: Portal protein of full Haloferax tailed virus 1. Method: EM (single particle) / Resolution: 2.342 Å 18633 8qsi EMDB-18633, PDB-8qsi: Portal protein of empty Haloferax tailed virus 1. Method: EM (single particle) / Resolution: 2.75 Å 18642 8qsy EMDB-18642, PDB-8qsy: Portal capsid interface of full Haloferax tailed virus 1. Method: EM (single particle) / Resolution: 2.68 Å 50521 9fkb EMDB-50521, PDB-9fkb: Tail of emppty Haloferax tailed virus 1 Method: EM (single particle) / Resolution: 2.96 Å 51530 9gs0 EMDB-51530, PDB-9gs0: Capsid of full Haloferax tailed virus 1 without turret head protein gp31. Method: EM (single particle) / Resolution: 2.37 Å 51866 9h4p EMDB-51866, PDB-9h4p: Tail of full Haloferax tailed virus 1 Method: EM (single particle) / Resolution: 2.44 Å 51883 9h5b EMDB-51883, PDB-9h5b: Tail fibre of Haloferax tailed virus 1 Method: EM (single particle) / Resolution: 3.6 Å 51915 9h7v EMDB-51915, PDB-9h7v: The baseplate assembly of Haloferax tailed virus 1. Method: EM (single particle) / Resolution: 2.6 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry ChemComp-K: Unknown entry
Source	haloferax tailed virus 1
Keywords	VIRUS / Archeal virus / turret / turret capsid interface / Mg ions / Archaeal virus / portal / portal capsid interface / tail / capsid / baseplate / tape measure protein / tail fiber