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@INBOOK{Schlesinger:838453,
      author       = {Schlesinger, R. and Cousin, Anneliese and Granzin, Joachim
                      and Batra-Safferling, Renu},
      title        = {{E}xpression and purification of arrestin in yeast
                      {S}accharomyces cerevisiae},
      address      = {San Diego, US},
      publisher    = {Academic Press},
      reportid     = {FZJ-2017-07056},
      pages        = {159-172},
      year         = {2017},
      comment      = {Methods in Cell Biology - G Protein-Coupled Receptors},
      booktitle     = {Methods in Cell Biology - G
                       Protein-Coupled Receptors},
      abstract     = {Protein purity and yield are two critical parameters for
                      successful protein characterization using structural
                      techniques such as X-ray crystallography, NMR, and several
                      other biophysical methods. The yeast Saccharomyces
                      cerevisiae is one of the popular eukaryotic model systems
                      for overexpression and subsequent purification of
                      recombinant proteins. Here, we describe a protocol for
                      cloning, overexpression, purification, and crystallization
                      of arrestin-1 and its splice variant p44 from yeast. The
                      purification protocol involves a single-affinity
                      chromatography step on a Strep-Tactin column. Highly
                      purified arrestins can be concentrated up to 15 mg/mL using
                      ultrafiltration and can be stored in the frozen state for
                      several months without any loss of functionality.},
      cin          = {ICS-6},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)7},
      url          = {https://juser.fz-juelich.de/record/838453},
}