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@INPROCEEDINGS{Schrader:139570,
      author       = {Schrader, Tobias and Ostermann, Andreas and Monkenbusch,
                      Michael and Laatsch, Bernhard and Jüttner, Philipp and
                      Petry, Winfried and Richter, Dieter},
      title        = {{F}irst {R}esults from {M}easurements at the {N}ew{N}eutron
                      {D}iffractometer “{B}io{D}iff”},
      reportid     = {FZJ-2013-05553},
      year         = {2013},
      abstract     = {The neutron diffractometer BioDiff is a joint project
                      between the Forschungszentrum Jülich (FZJ/JCNS) and the
                      Forschungs-Neutronenquelle Heinz Maier-Leibnitz (FRM II).
                      The instrument BioDiff is especially designed to collect
                      data from crystals with large unit cells. The main field of
                      application is the structure analysis of proteins,
                      especially the determination of hydrogen atom positions.
                      Typical scientific questions addressed are the determination
                      of protonation states of amino acid side chains and the
                      characterization of the hydrogen bonding networks between
                      the protein and an inhibitor or substrate. The orientation
                      of water molecules in the active centre of the protein can
                      also be determined (c. f. Fig. 1). The main advantage of the
                      monochromatic instrument BioDiff is the possibility to adapt
                      the wavelength between 2.4 Å and 5.6 Å to obtain a
                      compromise between higher scattering yields at longer
                      wavelengths and better resolution at smaller wavelengths. In
                      this contribution the most recent results from the
                      instrument BioDiff will be presented concentrating on the
                      recently published measurements on the Toho-1 -lactamase
                      mutant R274N/R276N [1] and on myoglobin crystals [2]. The
                      latter example will be given because it shows that data from
                      BioDiff can be compared to similar instruments e. g. the
                      BIX-3 in Japan. Here, the water network around the outer
                      surface of the protein was investigated. Figure 1 nicely
                      shows how the orientation of water molecules can be
                      determined on the surface of the protein if the water
                      molecules are fixed well enough due to a surrounding
                      hydrogen bonding network.},
      month         = {Aug},
      date          = {2013-08-25},
      organization  = {The 28th Meeting of the European
                       Crystallographic Association, Warwick
                       (United Kingdom), 25 Aug 2013 - 29 Aug
                       2013},
      cin          = {JCNS-1 / JCNS (München) ; Jülich Centre for Neutron
                      Science JCNS (München) ; JCNS-FRM-II / ICS-1},
      cid          = {I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)ICS-1-20110106},
      pnm          = {451 - Soft Matter Composites (POF2-451) / 54G - JCNS
                      (POF2-54G24)},
      pid          = {G:(DE-HGF)POF2-451 / G:(DE-HGF)POF2-54G24},
      typ          = {PUB:(DE-HGF)24},
      url          = {https://juser.fz-juelich.de/record/139570},
}