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@ARTICLE{Kkolu:1031216,
      author       = {Küçükoğlu, Berk and Mohammed, Inayathulla and
                      Guerrero-Ferreira, Ricardo C. and Ribet, Stephanie M. and
                      Varnavides, Georgios and Leidl, Max Leo and Lau, Kelvin and
                      Nazarov, Sergey and Myasnikov, Alexander and Kube, Massimo
                      and Radecke, Julika and Sachse, Carsten and Müller-Caspary,
                      Knut and Ophus, Colin and Stahlberg, Henning},
      title        = {{L}ow-dose cryo-electron ptychography of proteins at
                      sub-nanometer resolution},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2024-05612},
      pages        = {8062},
      year         = {2024},
      abstract     = {Cryo-transmission electron microscopy (cryo-EM) of frozen
                      hydrated specimens is an efficient method for the structural
                      analysis of purified biological molecules. However, cryo-EM
                      and cryo-electron tomography are limited by the low
                      signal-to-noise ratio (SNR) of recorded images, making
                      detection of smaller particles challenging. For
                      dose-resilient samples often studied in the physical
                      sciences, electron ptychography – a coherent diffractive
                      imaging technique using 4D scanning transmission electron
                      microscopy (4D-STEM) – has recently demonstrated excellent
                      SNR and resolution down to tens of picometers for thin
                      specimens imaged at room temperature. Here we apply 4D-STEM
                      and ptychographic data analysis to frozen hydrated proteins,
                      reaching sub-nanometer resolution 3D reconstructions. We
                      employ low-dose cryo-EM with an aberration-corrected,
                      convergent electron beam to collect 4D-STEM data for our
                      reconstructions. The high frame rate of the electron
                      detector allows us to record large datasets of electron
                      diffraction patterns with substantial overlaps between the
                      interaction volumes of adjacent scan positions, from which
                      the scattering potentials of the samples are iteratively
                      reconstructed. The reconstructed micrographs show strong SNR
                      enabling the reconstruction of the structure of apoferritin
                      protein at up to 5.8 Å resolution. We also show
                      structural analysis of the Phi92 capsid and sheath, tobacco
                      mosaic virus, and bacteriorhodopsin at slightly lower
                      resolutions.},
      cin          = {ER-C-3},
      ddc          = {500},
      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) /
                      4D-BioSTEM (DE002325)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241 /
                      G:(DE-Juel-1)DE002325},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39277607},
      UT           = {WOS:001457649000008},
      doi          = {10.1038/s41467-024-52403-5},
      url          = {https://juser.fz-juelich.de/record/1031216},
}