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@INPROCEEDINGS{Schrader:873034,
      author       = {Schrader, Tobias Erich and Ostermann, Andreas and
                      Monkenbusch, Michael and Laatsch, Bernhard and Jüttner,
                      Philipp and Petry, Winfried and Richter, Dieter},
      title        = {{N}eutron protein crystallography at the {H}einz
                      {M}aier-{L}eibnitz {Z}entrum ({MLZ}): {N}ew developments and
                      recent application examples},
      reportid     = {FZJ-2020-00485},
      year         = {2019},
      abstract     = {The neutron single crystal diffractometer BIODIFF at the
                      research reactor Heinz Maier-Leibnitz (FRM II) is especially
                      designed to collect data from crystals with large unit
                      cells. The main field of application is the structural
                      analysis of proteins, especially the determination of
                      hydrogen atom positions. BIODIFF is a joint project of the
                      Jülich Centre for Neutron Science (JCNS) and the FRM II.
                      BIODIFF is designed as a monochromatic instrument with a
                      narrow wavelength spread of less than 3 $\%.$ To cover a
                      large solid angle the main detector of BIODIFF consists of a
                      neutron imaging plate in a cylindrical geometry with online
                      read-out capability. BIODFF is equipped with a standard
                      Oxford Cryosystem “Cryostream 700+” which allows
                      measurements at 100 K. A new kappa goniometer head was added
                      recently. This allows an automated tilting of the crystal in
                      order to increase the completeness of the data set when
                      recording another set of frames in the tilted geometry.
                      Typical scientific questions addressed are the determination
                      of protonation states of amino acid side chains in proteins
                      and the characterization of the hydrogen bonding networks
                      between the protein active centre and an inhibitor or
                      substrate. Picking out some recent highlights from
                      measurements at BIODIFF it will be shown how the method of
                      neutron protein crystallography could be used to answer
                      mechanistic questions in enzymatic processes or help to
                      improve inhibitor fragment screening.},
      month         = {Aug},
      date          = {2019-08-18},
      organization  = {ECM, Wien (Austria), 18 Aug 2019 - 18
                       Aug 2019},
      subtyp        = {After Call},
      cin          = {JCNS-FRM-II / JCNS-1 / JCNS-2 / ZEA-1 / MLZ},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106 /
                      I:(DE-Juel1)ZEA-1-20090406 / I:(DE-588b)4597118-3},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)24},
      url          = {https://juser.fz-juelich.de/record/873034},
}