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@ARTICLE{Maurer:613832,
      author       = {Maurer, Valentin J. and Siggel, Marc and Kosinski, Jan},
      title        = {{W}hat shapes template-matching performance in cryogenic
                      electron tomography in situ?},
      journal      = {Acta crystallographica / Section D},
      volume       = {80},
      number       = {6},
      issn         = {2059-7983},
      address      = {Bognor Regis},
      publisher    = {Wiley},
      reportid     = {PUBDB-2024-05638},
      pages        = {410-420},
      year         = {2024},
      abstract     = {The detection of specific biological macromolecules in
                      cryogenic electron tomography data is frequently approached
                      by applying cross-correlation-based 3D template matching. To
                      reduce computational cost and noise, high binning is used to
                      aggregate voxels before template matching. This remains a
                      prevalent practice in both practical applications and
                      methods development. Here, the relation between template
                      size, shape and angular sampling is systematically evaluated
                      to identify ribosomes in a ground-truth annotated data set.
                      It is shown that at the commonly used binning, a detailed
                      subtomogram average, a sphere and a heart emoji result in
                      near-identical performance. These findings indicate that
                      with current template-matching practices macromolecules can
                      only be detected with high precision if their shape and size
                      are sufficiently different from the background. Using
                      theoretical considerations, the experimental results are
                      rationalized and it is discussed why primarily low-frequency
                      information remains at high binning and that template
                      matching fails to be accurate because similarly shaped and
                      sized macromolecules have similar low-frequency spectra.
                      These challenges are discussed and potential enhancements
                      for future template-matching methodologies are proposed.},
      cin          = {CSSB-EMBL-JK},
      ddc          = {530},
      cid          = {I:(DE-H253)CSSB-EMBL-JK-20210701},
      pnm          = {899 - ohne Topic (POF4-899) / EIPOD4 - EMBL
                      Interdisciplinary Postdoc Programme 4 (847543)},
      pid          = {G:(DE-HGF)POF4-899 / G:(EU-Grant)847543},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38805246},
      UT           = {WOS:001257892800004},
      doi          = {10.1107/S2059798324004303},
      url          = {https://bib-pubdb1.desy.de/record/613832},
}