% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Leidl:1050257,
      author       = {Leidl, Max Leo and Sturm, Sebastian and Filopoulou,
                      Aikaterina and Sachse, Carsten and Müller-Caspary, Knut},
      title        = {{T}owards a {P}rotein-{S}ize {D}ependent {R}esolution
                      {L}imit due to {D}ynamical {S}cattering in
                      {C}ryo-transmission {E}lectron {M}icroscopy},
      journal      = {Microscopy and microanalysis},
      volume       = {31},
      number       = {6},
      issn         = {1079-8501},
      address      = {Oxford},
      publisher    = {Oxford University Press},
      reportid     = {FZJ-2026-00069},
      pages        = {ozaf123},
      year         = {2025},
      abstract     = {In cryo-transmission electron microscopy, single-particle
                      reconstructions exploit the weak phase object approximation.
                      A decisive aspect to be studied systematically is to what
                      extent underlying scattering assumptions limit the
                      resolution, whether theoretical limits are compatible with
                      experimental observations, and if current experimental
                      benchmarks achieve this limit. Single-, multislice, and
                      hybrid scattering models are employed in this work for
                      simulating eight protein complexes up to 97.5 nm in
                      thickness, embedded in low-density amorphous ice obtained
                      from molecular dynamics. With the multislice scheme
                      providing an accurate solution to the multiple scattering
                      problem as reference, the reliability of the different
                      models is assessed in both real and Fourier space,
                      particularly via Fourier ring correlations at the specimen
                      exit wave level. A comparison with benchmarking literature
                      resolutions is performed. Our results show proportionality
                      of the attainable resolution to the square root of the
                      projection thickness. This is in reasonable quantitative
                      agreement with the highest resolution published
                      experimentally for proteins with at least the size of
                      apoferritin. The study provides a rationale for the
                      expectable resolution for a protein complex of known size.
                      The implications of structural noise due to the ice
                      background for the minimal ice thickness on protein
                      size-dependent resolution are discussed, as well as
                      efficient methods to approximate multiple scattering and
                      propagation in thick proteins.},
      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},
      doi          = {10.1093/mam/ozaf123},
      url          = {https://juser.fz-juelich.de/record/1050257},
}