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@INPROCEEDINGS{Schrader:848775,
      author       = {Schrader, Tobias Erich and Ostermann and Monkenbusch,
                      Michael and Laatsch, Bernhard and Jüttner, Ph. and Petry,
                      Winfried and Richter, Dieter},
      title        = {{N}eutron protein crystallography: {N}ew developments and
                      recent application examples},
      reportid     = {FZJ-2018-03710},
      year         = {2017},
      abstract     = {With the advent of new instruments (e. g. Imagine at HFIR,
                      MANDI at SNS and BIODIFF at FRMII) and well established
                      instruments (iBIX at JPARC and LADI at ILL) neutron protein
                      crystallography has seen a resurrection from the past
                      pioneering work by Schoenborn. New sample environment
                      options at the instruments and a growing user community have
                      greatly enhanced the outcome of the existing neutron
                      diffractometers. Measurements at 100 K in a nitrogen gas
                      stream (cryostream) are now routinely possible at most
                      neutron diffractometers. Efforts to increase the flux at the
                      sample position and to reduce the background at the detector
                      enable to measure smaller and smaller protein crystals. Yet,
                      measuring crystals with volumes below 0.1 mm3 is still a big
                      challenge and usually works only in exceptional cases. The
                      main scientific questions addressed are: Hydrogen bonding to
                      ligands/substrates, protonation states of amino acids in
                      intermediate states of the catalytic process and determining
                      the correct structure of metallo-proteins which are
                      subjected to reduction due to the radiation damage caused by
                      x-rays. But also the water shell on the outer surface of the
                      protein can be studied, whereby water molecules of different
                      flexibility can be observed.As an example for a neutron
                      diffractometer, the instrument BIODIFF is introduced: It 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. An
                      optical CCD-camera pointing at the sample position is used
                      to quickly align the sample (or a Cadmium replica of it)
                      with respect to the neutron beam. The main advantage of
                      BIODIFF is the possibility to adapt the wavelength to the
                      size of the unit cell of the sample crystal while operating
                      with a clean monochromatic beam that keeps the background
                      level low.In this contribution, a review of most recent
                      application examples of neutron protein crystallography is
                      given. New developments are discussed which may lead to a
                      widening of the application scope of this method. Especially
                      the need for large protein (typically > 0.5 mm3 in volume)
                      crystals is addressed.},
      month         = {May},
      date          = {2017-05-24},
      organization  = {Instruct Biennial Structural Biology
                       Conference 2017, Brno (Czech Republic),
                       24 May 2017 - 26 May 2017},
      subtyp        = {Outreach},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1 /
                      ZEA-1 / JCNS-2},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)ZEA-1-20090406 /
                      I:(DE-Juel1)JCNS-2-20110106},
      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/848775},
}