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@ARTICLE{Gati:317888,
      author       = {Gati, Cornelius and Oberthuer, Dominik and Yefanov,
                      Oleksandr and Bunker and Stellato, Francesco and chiu,
                      Elaine and Yeh, Shin-Mei and Aquila, Andrew and Basu, Shibom
                      and Bean, Richard and Beyerlein, Kenneth and Botha, Sabine
                      and Boutet, Sebastien and DePonte, Daniel and Doak, R. Bruce
                      and Fromme, Raimund and Galli, Lorenzo and grotjohan, Ingo
                      and James, Daniel and Kupitz, Christopher and Lomb, Lukas
                      and Messerschmidt, Marc and Nass, Karol and Rendek, Kimberly
                      and Shoeman, Robert and Wang, Dingjie and Weierstall, Uwe
                      and White, Thomas and Williams, Garth and Zatsepin, Nadia
                      and Fromme, Petra and Goldie, Kenneth and Jehle, Johannes
                      and Metcalf, Peter and Barty, Anton and Chapman, Henry N.},
      title        = {{A}tomic {S}tructure of {G}ranulin {D}etermined from
                      {N}ative {N}anocrystalline {G}ranulovirus {U}sing an {X}-ray
                      {F}ree-{E}lectron {L}aser},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {114},
      number       = {9},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {PUBDB-2017-00953},
      pages        = {2247 – 2252},
      year         = {2017},
      note         = {© National Academy of Sciences},
      abstract     = {To understand how molecules function in biological systems,
                      new methods are required to obtain atomic resolution
                      structures from biological material under physiological
                      conditions. Intense femtosecond-duration pulses from X-ray
                      free-electron lasers (XFELs) can outrun most damage
                      processes, vastly increasing the tolerable dose before the
                      specimen is destroyed. This in turn allows structure
                      determination from crystals much smaller and more radiation
                      sensitive than previously considered possible, allowing data
                      collection from room temperature structures and avoiding
                      structural changes due to cooling. Regardless,
                      high-resolution structures obtained from XFEL data mostly
                      use crystals far larger than 1 μm$^3$ in volume, whereas
                      the X-ray beam is often attenuated to protect the detector
                      from damage caused by intense Bragg spots. Here, we describe
                      the 2 Å resolution structure of native nanocrystalline
                      granulovirus occlusion bodies (OBs) that are less than 0.016
                      μm$^3$ in volume using the full power of the Linac Coherent
                      Light Source (LCLS) and a dose up to 1.3 GGy per crystal.
                      The crystalline shell of granulovirus OBs consists, on
                      average, of about 9,000 unit cells, representing the
                      smallest protein crystals to yield a high-resolution
                      structure by X-ray crystallography to date. The XFEL
                      structure shows little to no evidence of radiation damage
                      and is more complete than a model determined using
                      synchrotron data from recombinantly produced, much larger,
                      cryocooled granulovirus granulin microcrystals. Our
                      measurements suggest that it should be possible, under ideal
                      experimental conditions, to obtain data from protein
                      crystals with only 100 unit cells in volume using currently
                      available XFELs and suggest that single-molecule imaging of
                      individual biomolecules could almost be within reach.},
      cin          = {CFEL-I / Eur.XFEL / UNI/CUI / CFEL-QCM / ASU},
      ddc          = {000},
      cid          = {I:(DE-H253)CFEL-I-20161114 / $I:(DE-H253)Eur_XFEL-20120731$
                      / $I:(DE-H253)UNI_CUI-20121230$ /
                      I:(DE-H253)CFEL-QCM-20160914 / I:(DE-H253)ASU-20151130},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      Leibniz Preis - Leibiz Programm 2015: Prof. Dr. Henry N.
                      Chapman (DFG-Leibniz-2015-Chapman) / VH-GS-500 - PIER
                      Helmholtz Graduate School $(2015_IFV-VH-GS-500)$},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-H253)DFG-Leibniz-2015-Chapman /
                      $G:(DE-HGF)2015_IFV-VH-GS-500$},
      experiment   = {EXP:(DE-H253)CFEL-Exp-20150101 /
                      EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000395101200053},
      pubmed       = {pmid:28202732},
      doi          = {10.1073/pnas.1609243114},
      url          = {https://bib-pubdb1.desy.de/record/317888},
}