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@ARTICLE{Gushchin:874733,
      author       = {Gushchin, Ivan and Melnikov, Igor and Polovinkin, Vitaly
                      and Ishchenko, Andrii and Gordeliy, Valentin},
      title        = {{C}rystal {S}tructure of a {P}roteolytic {F}ragment of the
                      {S}ensor {H}istidine {K}inase {N}ar{Q}},
      journal      = {Crystals},
      volume       = {10},
      number       = {3},
      issn         = {2073-4352},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2020-01642},
      pages        = {149 -},
      year         = {2020},
      abstract     = {Two-component signaling systems (TCSs) are a large and
                      important class of sensory systems in bacteria, archaea, and
                      some eukaryotes, yet their mechanism of action is still not
                      fully understood from the structural point of view. Many TCS
                      receptors are elongated flexible proteins with transmembrane
                      (TM) regions, and are difficult to work with. Consequently,
                      truncated fragments of the receptors are often used in
                      structural studies. However, it is not fully clear whether
                      the structures of the fragments correspond well to their
                      native structures in the context of full-length proteins.
                      Recently, we crystallized a fragment of Escherichia coli
                      nitrate/nitrite sensor histidine kinase, NarQ, encompassing
                      the sensor, TM, and HAMP domains. Here we report that a
                      smaller proteolytic fragment consisting of the sensor and TM
                      domains can also be crystallized using the in meso approach.
                      The structure of the fragment is similar to the previously
                      determined one, with minor differences in the vicinity of
                      the truncation site. The results show that the
                      crystallization of such sensor–TM fragments can be
                      accomplished and can provide information on the packing of
                      transmembrane helices, albeit limited, and that the
                      proteolysis may or may not be a problem during
                      crystallization.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000523512100051},
      doi          = {10.3390/cryst10030149},
      url          = {https://juser.fz-juelich.de/record/874733},
}