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@ARTICLE{Ryzhykau:902966,
      author       = {Ryzhykau, Yury L. and Vlasov, Alexey V. and Orekhov,
                      Philipp S. and Rulev, Maksim I. and Rogachev, Andrey V. and
                      Vlasova, Anastasia D. and Kazantsev, Alexander S. and
                      Verteletskiy, Dmitry P. and Skoi, Vadim V. and Brennich,
                      Martha E. and Pernot, Petra and Murugova, Tatiana N. and
                      Gordeliy, Valentin I. and Kuklin, Alexander I.},
      title        = {{A}mbiguities in and completeness of {SAS} data analysis of
                      membrane proteins: the case of the sensory rhodopsin
                      {II}–transducer complex},
      journal      = {Acta crystallographica / Section D},
      volume       = {77},
      number       = {11},
      issn         = {0907-4449},
      address      = {Bognor Regis},
      publisher    = {Wiley},
      reportid     = {FZJ-2021-04712},
      pages        = {1386 - 1400},
      year         = {2021},
      abstract     = {Membrane proteins (MPs) play vital roles in the function of
                      cells and are also major drug targets. Structural
                      information on proteins is vital for understanding their
                      mechanism of function and is critical for the development of
                      drugs. However, obtaining high-resolution structures of
                      membrane proteins, in particular, under native conditions is
                      still a great challenge. In such cases, the low-resolution
                      methods small-angle X-ray and neutron scattering (SAXS and
                      SANS) might provide valuable structural information.
                      However, in some cases small-angle scattering (SAS) provides
                      ambiguous ab initio structural information if complementary
                      measurements are not performed and/or a priori information
                      on the protein is not taken into account. Understanding the
                      nature of the limitations may help to overcome these
                      problems. One of the main problems of SAS data analysis of
                      solubilized membrane proteins is the contribution of the
                      detergent belt surrounding the MP. Here, a comprehensive
                      analysis of how the detergent belt contributes to the SAS
                      data of a membrane-protein complex of sensory rhodopsin II
                      with its cognate transducer from Natronomonas pharaonis
                      (NpSRII-NpHtrII) was performed. The influence of the
                      polydispersity of NpSRII-NpHtrII oligomerization is the
                      second problem that is addressed here. It is shown that
                      inhomogeneity in the scattering length density of the
                      detergent belt surrounding a membrane part of the complex
                      and oligomerization polydispersity significantly impacts on
                      SAXS and SANS profiles, and therefore on 3D ab initio
                      structures. It is described how both problems can be taken
                      into account to improve the quality of SAS data treatment.
                      Since SAS data for MPs are usually obtained from solubilized
                      proteins, and their detergent belt and, to a certain extent,
                      oligomerization polydispersity are sufficiently common
                      phenomena, the approaches proposed in this work might be
                      used in SAS studies of different MPs.},
      cin          = {IBI-7},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34726167},
      UT           = {WOS:000714429000006},
      doi          = {10.1107/S2059798321009542},
      url          = {https://juser.fz-juelich.de/record/902966},
}