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@ARTICLE{Ekeberg:599083,
      author       = {Ekeberg, Tomas and Assalauova, Dameli and Bielecki, Johan
                      and Boll, Rebecca and Daurer, Benedikt J. and Eichacker,
                      Lutz A. and Franken, Linda E. and Galli, Davide E. and
                      Gelisio, Luca and Gumprecht, Lars and Gunn, Laura H. and
                      Hajdu, Janos and Hartmann, Robert and Hasse, Dirk and
                      Ignatenko, Alexandr and Koliyadu, Jayanath and Kulyk, Olena
                      and Kurta, Ruslan and Kuster, Markus and Lugmayr, Wolfgang
                      and Lübke, Jannik and Mancuso, Adrian P. and Mazza, Tommaso
                      and Nettelblad, Carl and Ovcharenko, Yevheniy and Rivas,
                      Daniel E. and Samanta, Amit K. and Schmidt, Philipp and
                      Sobolev, Egor and Timneanu, Nicusor and Usenko, Sergej and
                      Westphal, Daniel and Wollweber, Tamme and Worbs, Lena and
                      Xavier, P. Lourdu and Yousef, Hazem and Ayyer, Kartik and
                      Chapman, Henry N. and Sellberg, Jonas A. and Seuring,
                      Carolin and Vartanyants, Ivan A. and Küpper, Jochen and
                      Meyer, Michael and Maia, Filipe R. N. C.},
      title        = {{O}bservation of a single protein by ultrafast {X}-ray
                      diffraction},
      reportid     = {PUBDB-2023-07149},
      year         = {2023},
      note         = {The paper is accepted for publication in Light: Science
                      $\&$ Applications but not published yet. Information from
                      Amit Samanta.},
      abstract     = {The idea of using ultrashort X-ray pulses to obtain images
                      of single proteins frozen in time has fascinated and
                      inspired many. It was one of the arguments for building
                      X-ray free-electron lasers. According to theory1, the
                      extremely intense pulses provide sufficient signal to
                      dispense with using crystals as an amplifier, and the
                      ultrashort pulse duration permits capturing the diffraction
                      data before the sample inevitably explodes2. This was first
                      demonstrated on biological samples a decade ago on the giant
                      mimivirus3. Since then a large collaboration4 has been
                      pushing the limit of the smallest sample that can be
                      imaged5,6. The ability to capture snapshots on the timescale
                      of atomic vibrations, while keeping the sample at room
                      temperature, may allow probing the entire conformational
                      phase space of macromolecules. Here we show the first
                      observation of an X-ray diffraction pattern from a single
                      protein, that of Escherichia coli GroEL which at 14 nm in
                      diameter7 is the smallest biological sample ever imaged by
                      X-rays, and demonstrate that the concept of diffraction
                      before destruction extends to single proteins. From the
                      pattern, it is possible to determine the approximate
                      orientation of the protein. Our experiment demonstrates the
                      feasibility of ultrafast imaging of single proteins, opening
                      the way to single-molecule time-resolved studies on the
                      femtosecond timescale.},
      cin          = {FS-CFEL-CMI / FS-CFEL-1 / UNI/CUI / UNI/EXP / FS-PS},
      cid          = {I:(DE-H253)FS-CFEL-CMI-20220405 /
                      I:(DE-H253)FS-CFEL-1-20120731 /
                      $I:(DE-H253)UNI_CUI-20121230$ /
                      $I:(DE-H253)UNI_EXP-20120731$ / I:(DE-H253)FS-PS-20131107},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / DFG project 390715994 - EXC 2056:
                      CUI: Advanced Imaging of Matter (390715994) / COMOTION -
                      Controlling the Motion of Complex Molecules and Particles
                      (614507) / Leibniz Preis - Leibiz Programm 2015: Prof. Dr.
                      Henry N. Chapman (DFG-Leibniz-2015-Chapman) / 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)POF4-633 / G:(GEPRIS)390715994 /
                      G:(EU-Grant)614507 / G:(DE-H253)DFG-Leibniz-2015-Chapman /
                      G:(GEPRIS)194651731},
      experiment   = {EXP:(DE-H253)XFEL-Exp-20150101 /
                      EXP:(DE-H253)CFEL-Exp-20150101},
      typ          = {PUB:(DE-HGF)25},
      doi          = {10.1101/2022.03.09.483477},
      url          = {https://bib-pubdb1.desy.de/record/599083},
}