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@ARTICLE{Midtgaard:841071,
      author       = {Midtgaard, Søren Roi and Darwish, Tamim A. and Pedersen,
                      Martin Cramer and Huda, Pie and Larsen, Andreas Haahr and
                      Jensen, Grethe Vestergaard and Kynde, Søren Andreas Røssel
                      and Skar-Gislinge, Nicholas and Nielsen, Agnieszka Janina
                      Zygadlo and Olesen, Claus and Blaise, Mickael and Dorosz,
                      Jerzy Józef and Thorsen, Thor Seneca and Venskutonytė,
                      Raminta and Krintel, Christian and Møller, Jesper V. and
                      Frielinghaus, Henrich and Gilbert, Elliot Paul and Martel,
                      Anne and Kastrup, Jette Sandholm and Jensen, Poul Erik and
                      Nissen, Poul and Arleth, Lise},
      title        = {{I}nvisible detergents for structure determination of
                      membrane proteins by small-angle neutron scattering},
      journal      = {The FEBS journal},
      volume       = {285},
      number       = {2},
      issn         = {1742-464X},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2017-08171},
      pages        = {357–371},
      year         = {2018},
      abstract     = {A novel and generally applicable method for determining
                      structures of membrane proteins in solution via small-angle
                      neutron scattering (SANS) is presented. Common detergents
                      for solubilizing membrane proteins were synthesized in
                      isotope-substituted versions for utilizing the intrinsic
                      neutron scattering length difference between hydrogen and
                      deuterium. Individual hydrogen/deuterium levels of the
                      detergent head and tail groups were achieved such that the
                      formed micelles became effectively invisible in heavy water
                      (D2O) when investigated by neutrons. This way, only the
                      signal from the membrane protein remained in the SANS data.
                      We demonstrate that the method is not only generally
                      applicable on five very different membrane proteins but also
                      reveals subtle structural details about the
                      sarco/endoplasmatic reticulum Ca2+ ATPase (SERCA). In all,
                      the synthesis of isotope-substituted detergents makes
                      solution structure determination of membrane proteins bySANS
                      and subsequent data analysis available to non-specialists.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29178440},
      UT           = {WOS:000423416700011},
      doi          = {10.1111/febs.14345},
      url          = {https://juser.fz-juelich.de/record/841071},
}