000889727 001__ 889727 000889727 005__ 20210208142347.0 000889727 0247_ $$2doi$$a10.1038/s41467-020-19611-1 000889727 0247_ $$2Handle$$a2128/26805 000889727 0247_ $$2altmetric$$aaltmetric:94204160 000889727 0247_ $$2pmid$$a33188213 000889727 0247_ $$2WOS$$aWOS:000594647500010 000889727 037__ $$aFZJ-2021-00348 000889727 082__ $$a500 000889727 1001_ $$0P:(DE-HGF)0$$aZinke, Maximilian$$b0 000889727 245__ $$aArchitecture of the flexible tail tube of bacteriophage SPP1 000889727 260__ $$a[London]$$bNature Publishing Group UK$$c2020 000889727 3367_ $$2DRIVER$$aarticle 000889727 3367_ $$2DataCite$$aOutput Types/Journal article 000889727 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1610982640_12015 000889727 3367_ $$2BibTeX$$aARTICLE 000889727 3367_ $$2ORCID$$aJOURNAL_ARTICLE 000889727 3367_ $$00$$2EndNote$$aJournal Article 000889727 520__ $$aBacteriophage SPP1 is a double-stranded DNA virus of the Siphoviridae family that infects the bacterium Bacillus subtilis. This family of phages features a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, we present the atomic structure of the tail tube of phage SPP1. Our hybrid structure is based on the integration of structural restraints from solid-state nuclear magnetic resonance (NMR) and a density map from cryo-EM. We show that the tail tube protein gp17.1 organizes into hexameric rings that are stacked by flexible linker domains and, thus, form a hollow flexible tube with a negatively charged lumen suitable for the transport of DNA. Additionally, we assess the dynamics of the system by combining relaxation measurements with variances in density maps. 000889727 536__ $$0G:(DE-HGF)POF3-551$$a551 - Functional Macromolecules and Complexes (POF3-551)$$cPOF3-551$$fPOF III$$x0 000889727 588__ $$aDataset connected to CrossRef 000889727 7001_ $$00000-0002-5154-5217$$aSachowsky, Katrin A. 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