% 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”.

@ARTICLE{Coates:188456,
      author       = {Coates, Leighton and Tomanicek, Stephen and Schrader,
                      Tobias E. and Weiss, Kevin L. and Ng, Joseph D. and
                      Jüttner, Philipp and Ostermann, Andreas},
      title        = {{C}ryogenic neutron protein crystallography: routine
                      methods and potential benefits},
      journal      = {Journal of applied crystallography},
      volume       = {47},
      number       = {4},
      issn         = {1600-5767},
      address      = {Copenhagen},
      publisher    = {Munksgaard},
      reportid     = {FZJ-2015-01832},
      pages        = {1431 - 1434},
      year         = {2014},
      abstract     = {The use of cryocooling in neutron diffraction has been
                      hampered by several technical challenges, such as the need
                      for specialized equipment and techniques. This article
                      reports the recent development and deployment of equipment
                      and strategies that allow routine neutron data collection on
                      cryocooled crystals using off-the-shelf components. This
                      system has several advantages compared to a closed displex
                      cooling system, such as fast cooling coupled with easier
                      crystal mounting and centering. The ability to routinely
                      collect cryogenic neutron data for analysis will
                      significantly broaden the range of scientific questions that
                      can be examined by neutron protein crystallography.
                      Cryogenic neutron data collection for macromolecules has
                      recently become available at the new Biological
                      Diffractometer BIODIFF at the FRM II and the Macromolecular
                      Diffractometer (MaNDi) at the Spallation Neutron Source, Oak
                      Ridge National Laboratory. To evaluate the benefits of a
                      cryocooled neutron structure, a full neutron data set was
                      collected on the BIODIFF instrument on a Toho-1
                      [beta]-lactamase structure at 100 K.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {54G - JCNS (POF2-54G24)},
      pid          = {G:(DE-HGF)POF2-54G24},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000340362000030},
      doi          = {10.1107/S1600576714010772},
      url          = {https://juser.fz-juelich.de/record/188456},
}