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@PHDTHESIS{Roedig:331060,
      author       = {Roedig, Philip},
      othercontributors = {Weckert, Edgar and Chapman, Henry N.},
      title        = {{A} {N}ew {F}ixed-{T}arget {A}pproach for {S}erial
                      {C}rystallography at {S}ynchrotron {L}ight {S}ources and
                      {X}-ray {F}ree {E}lectron {L}asers},
      school       = {Universität Hamburg},
      type         = {Dr.},
      address      = {Hamburg},
      publisher    = {Verlag Deutsches Elektronen-Synchrotron},
      reportid     = {PUBDB-2017-07483, DESY-THESIS-2017-027},
      series       = {DESY-THESIS},
      pages        = {185},
      year         = {2017},
      note         = {Universität Hamburg, Diss., 2016},
      abstract     = {In the framework of this thesis, a new method for
                      high-speed fixed-target serial crystallography experiments
                      and its applicability to biomacromolecular crystallography
                      at both synchrotron light sources and X-ray free electron
                      lasers (XFELs) is presented. The method is based on a sample
                      holder, which can carry up to 20,000 microcrystals and which
                      is made of single-crystalline silicon. Using synchrotron
                      radiation, the structure of Operophtera brumata cytoplasmic
                      polyhedrosis virus type 18 polyhedrin, lysozyme and cubic
                      insulin was determined by collecting X-ray diffraction data
                      from multiple microcrystals. Data collection was shown to be
                      possible at both cryogenic and ambient conditions. For
                      room-temperature measurements, both global and specific
                      indications of radiation damage were investigated and
                      characterized. Due to the sieve-like structure of the chip,
                      the microcrystals tend to arrange themselves according to
                      the micropore pattern, which allows for efficient sampling
                      of the sample material. In combination with a high-speed
                      scanning stage, the sample holder was furthermore shown to
                      be highly suitable for serial femtosecond crystallography
                      experiments. By fast raster scanning of the chip through the
                      pulsed X-ray beam of an XFEL, structure determination of a
                      virus, using the example of bovine enterovirus type 2, has
                      been demonstrated at an XFEL for the first time. Hit rates
                      of up to $100\%$ were obtained by the presented method,
                      which refers to a reduction in sample consumption by at
                      least three orders of magnitude with respect to common
                      liquid-jet injection methods used for sample delivery. In
                      this way, the typical time needed for data collection in
                      serial femtosecond crystallography is significantly
                      decreased. The presented technique for sample loading of the
                      chip is easy to learn and results in efficient removal of
                      the surrounding mother liquor, thereby reducing the
                      generated background signal. Since the chip is made of
                      single-crystalline silicon, in principle no diffuse
                      background contribution is caused by the chip itself.},
      cin          = {FS-PS},
      cid          = {I:(DE-H253)FS-PS-20131107},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)3 / PUB:(DE-HGF)29 / PUB:(DE-HGF)11},
      doi          = {10.3204/PUBDB-2017-07483},
      url          = {https://bib-pubdb1.desy.de/record/331060},
}