% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@INPROCEEDINGS{Schrader:860659,
      author       = {Schrader, Tobias Erich},
      title        = {{N}eutron protein crystallography: {N}ew developments and
                      recent application examples},
      school       = {Universität Wien},
      reportid     = {FZJ-2019-01327},
      year         = {2018},
      abstract     = {With the advent of new instruments (e. g. Imagine at HFIR,
                      MANDI at SNS and BIODIFF at FRMII) neutron protein
                      crystallography has seen a resurrection from the past
                      pioneering work by Goldstein et al. A growing user community
                      has greatly enhanced the outcome of the existing neutron
                      diffractometers specialized on protein crystallography.
                      Measurements at 100 K are now routinely possible at many
                      neutron diffractometers. Efforts to increase the flux at the
                      sample position and to reduce the background at the detector
                      push the limit of crystal volumes down to 0.1 mm3. The
                      neutron single crystal diffractometer BIODIFF at the
                      research reactor Heinz Maier-Leibnitz (FRM II) is 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
                      $\%$ where the central wavelength can be adapted between 2.7
                      and 5.6 Å. Some typical application examples to illustrate
                      the power of neutron protein crystallography will be given.
                      Time permitting I will report on two of my own research
                      projects. In one collaboration with the TUM engineering
                      department we try to optimize the crystallization of the
                      protein Alcoholdehydrogenase (ADH) by mutations on the
                      solvent exposed surface of the protein. The thermodynamic
                      effects on the crystal stability are simulated with all-atom
                      MD-simulations. The MD-results will be compared to the
                      actually observed crystallization behaviour of these
                      mutants. In a second project a crystallization apparatus is
                      developed which starts where the crystallization for x-ray
                      sized crystals ends: At a tiny crystal and known
                      crystallization conditions for it. The apparatus is intended
                      to be used to increase the size of this crystal by using it
                      as a seed crystal being put into a mother liquor containing
                      new supply of highly concentrated protein. Fine temperature
                      control and an optical control of the actual crystal size
                      will be provided with this apparatus. The idea behind this
                      apparatus is of course the growth of crystals which have a
                      sufficient volume for neutron protein crystallography.},
      month         = {Jun},
      date          = {2018-06-21},
      organization  = {Mondern Concepts Seminar, Universität
                       Wien, Wien (Austria), 21 Jun 2018 - 22
                       Jun 2018},
      subtyp        = {Invited},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      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)31},
      url          = {https://juser.fz-juelich.de/record/860659},
}