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@ARTICLE{Evans:1006587,
      author       = {Evans, Sasha L. and Al-Hazeem, Monsour M. J. and Mann,
                      Daniel and Smetacek, Nicolas and Beavil, Andrew J. and Sun,
                      Yaqi and Chen, Taiyu and Dykes, Gregory F. and Liu, Lu-Ning
                      and Bergeron, Julien R. C.},
      title        = {{S}ingle-particle cryo-{EM} analysis of the shell
                      architecture and internal organization of an intact
                      α-carboxysome},
      journal      = {Structure},
      volume       = {31},
      issn         = {0969-2126},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2023-01728},
      pages        = {S0969212623000849},
      year         = {2023},
      abstract     = {Carboxysomes are proteinaceous bacterial microcompartments
                      that sequester the key enzymes for carbon fixation in
                      cyanobacteria and some proteobacteria. They consist of a
                      virus-like icosahedral shell, encapsulating several enzymes,
                      including ribulose 1,5-bisphosphate carboxylase/oxygenase
                      (RuBisCO), responsible for the first step of the
                      Calvin-Benson-Bassham cycle. Despite their significance in
                      carbon fixation and great bioengineering potentials, the
                      structural understanding of native carboxysomes is currently
                      limited to low-resolution studies. Here, we report the
                      characterization of a native α-carboxysome from a marine
                      cyanobacterium by single-particle cryoelectron microscopy
                      (cryo-EM). We have determined the structure of its RuBisCO
                      enzyme, and obtained low-resolution maps of its icosahedral
                      shell, and of its concentric interior organization. Using
                      integrative modeling approaches, we have proposed a complete
                      atomic model of an intact carboxysome, providing insight
                      into its organization and assembly. This is critical for a
                      better understanding of the carbon fixation mechanism and
                      toward repurposing carboxysomes in synthetic biology for
                      biotechnological applications.},
      cin          = {ER-C-3},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37015227},
      UT           = {WOS:001012177900001},
      doi          = {10.1016/j.str.2023.03.008},
      url          = {https://juser.fz-juelich.de/record/1006587},
}