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@ARTICLE{Zinke:912262,
      author       = {Zinke, Maximilian and Schröder, Gunnar F. and Lange, Adam},
      title        = {{M}ajor tail proteins of bacteriophages of the order
                      {C}audovirales},
      journal      = {The journal of biological chemistry},
      volume       = {298},
      number       = {1},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2022-05459},
      pages        = {101472 -},
      year         = {2022},
      abstract     = {Technological advances in cryo-EM in recent years have
                      given rise to detailed atomic structures of bacteriophage
                      tail tubes—a class of filamentous protein assemblies that
                      could previously only be studied on the atomic scale in
                      either their monomeric form or when packed within a crystal
                      lattice. These hollow elongated protein structures, present
                      in most bacteriophages of the order Caudovirales, connect
                      the DNA-containing capsid with a receptor function at the
                      distal end of the tail and consist of helical and
                      polymerized major tail proteins. However, the resolution of
                      cryo-EM data for these systems differs enormously between
                      different tail tube types, partly inhibiting the building of
                      high-fidelity models and barring a combination with further
                      structural biology methods. Here, we review the structural
                      biology efforts within this field and highlight the role of
                      integrative structural biology approaches that have proved
                      successful for some of these systems. Finally, we summarize
                      the structural elements of major tail proteins and
                      conceptualize how different amounts of tail tube flexibility
                      confer heterogeneity within cryo-EM maps and, thus, limit
                      high-resolution reconstructions.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34890646},
      UT           = {WOS:000748376400016},
      doi          = {10.1016/j.jbc.2021.101472},
      url          = {https://juser.fz-juelich.de/record/912262},
}