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@ARTICLE{Koutsioumpas:840608,
      author       = {Koutsioumpas, Alexandros},
      title        = {{L}ow-{R}esolution {S}tructure of {D}etergent-{S}olubilized
                      {M}embrane {P}roteins from {S}mall-{A}ngle
                      {S}cattering {D}ata},
      journal      = {Biophysical journal},
      volume       = {113},
      number       = {11},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2017-08113},
      pages        = {2373 - 2382},
      year         = {2017},
      abstract     = {Despite the ever-increasing usage of small-angle scattering
                      as a valuable complementary method in the field of
                      structural biology, applications concerning membrane
                      proteins remain elusive mainly due to experimental
                      challenges and the relative lack of theoretical tools for
                      the treatment of scattering data. This fact adds up to
                      general difficulties encountered also by other established
                      methods (crystallography, NMR) for the study of membrane
                      proteins. Following the general paradigm of ab initio
                      methods for low-resolution restoration of soluble protein
                      structure from small-angle scattering data, we construct a
                      general multiphase model with a set of physical constraints,
                      which, together with an appropriate minimization procedure,
                      gives direct structural information concerning the different
                      components (protein, detergent molecules) of
                      detergent-solubilized membrane protein complexes. Assessment
                      of the method’s precision and robustness is evaluated by
                      performing shape restorations from simulated data of a
                      tetrameric α-helical membrane channel (Aquaporin-0)
                      solubilized by n-Dodecyl β-D-Maltoside and from previously
                      published small-angle neutron scattering experimental data
                      of the filamentous hemagglutinin adhesin β-barrel protein
                      transporter solubilized by n-Octyl β-D-glucopyranoside. It
                      is shown that the acquisition of small-angle neutron
                      scattering data at two different solvent contrasts, together
                      with an estimation of detergent aggregation number around
                      the protein, permits the reliable reconstruction of the
                      shape of membrane proteins without the need for any prior
                      structural information.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621) / 6G4 - Jülich Centre
                      for Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6215 /
                      G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29211991},
      UT           = {WOS:000417264300009},
      doi          = {10.1016/j.bpj.2017.10.003},
      url          = {https://juser.fz-juelich.de/record/840608},
}