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@ARTICLE{Bcker:435853,
      author       = {Bücker, Robert and Hogan-Lamarre, Pascal and Mehrabi,
                      Pedram and Schulz, Eike C. and Bultema, Lindsey A. and
                      Gevorkov, Yaroslav and Brehm, Wolfgang and Yefanov,
                      Oleksandr and Oberthür, Dominik and Kassier, Günther H.
                      and Miller, Dwayne},
      title        = {{S}erial protein crystallography in an electron microscope},
      journal      = {Nature Communications},
      volume       = {11},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2020-00822},
      pages        = {996},
      year         = {2020},
      note         = {open access},
      abstract     = {Serial X-ray crystallography at free-electron lasers allows
                      to solve biomolecular structures from sub-micron-sized
                      crystals. However, beam time at these facilities is scarce,
                      and involved sample delivery techniques are required. On the
                      other hand, rotation electron diffraction (MicroED) has
                      shown great potential as an alternative means for protein
                      nano-crystallography. Here, we present a method for serial
                      electron diffraction of protein nanocrystals combining the
                      benefits of both approaches. In a scanning transmission
                      electron microscope, crystals randomly dispersed on a sample
                      grid are automatically mapped, and a diffraction pattern at
                      fixed orientation is recorded from each at a high
                      acquisition rate. Dose fractionation ensures minimal
                      radiation damage effects. We demonstrate the method by
                      solving the structure of granulovirus occlusion bodies and
                      lysozyme to resolutions of 1.55 Å and 1.80 Å,
                      respectively. Our method promises to provide rapid structure
                      determination for many classes of materials with minimal
                      sample consumption, using readily available
                      instrumentation.},
      cin          = {CFEL-I / MPSD / CFEL-ARD / FS-CFEL-1},
      ddc          = {500},
      cid          = {I:(DE-H253)CFEL-I-20161114 / I:(DE-H253)MPSD-20120731 /
                      I:(DE-H253)CFEL-ARD-20160914 /
                      I:(DE-H253)FS-CFEL-1-20120731},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      AXSIS - Frontiers in Attosecond X-ray Science: Imaging and
                      Spectroscopy (609920) / DFG project 390715994 - EXC 2056:
                      CUI: Advanced Imaging of Matter (390715994) / DFG project
                      194651731 - EXC 1074: Hamburger Zentrum für ultraschnelle
                      Beobachtung (CUI): Struktur, Dynamik und Kontrolle von
                      Materie auf atomarer Skala (194651731)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(EU-Grant)609920 /
                      G:(GEPRIS)390715994 / G:(GEPRIS)194651731},
      experiment   = {EXP:(DE-H253)CFEL-Exp-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32081905},
      UT           = {WOS:000517991000002},
      doi          = {10.1038/s41467-020-14793-0},
      url          = {https://bib-pubdb1.desy.de/record/435853},
}