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@ARTICLE{Niebling:604257,
      author       = {Niebling, Stephan and Veith, Katharina and Vollmer,
                      Benjamin and Lizarrondo, Javier and Burastero, Osvaldo and
                      Schiller, Janina and Struve Garcia, Angelica and Lewe,
                      Philipp and Seuring, Carolin and Witt, Susanne and
                      García-Alai, María},
      title        = {{B}iophysical {S}creening {P}ipeline for {C}ryo-{EM} {G}rid
                      {P}reparation of {M}embrane {P}roteins},
      journal      = {Frontiers in molecular biosciences},
      volume       = {9},
      issn         = {2296-889X},
      address      = {Lausanne},
      publisher    = {Frontiers},
      reportid     = {PUBDB-2024-01055},
      pages        = {882288},
      year         = {2022},
      note         = {Part of this work was performed at the Cryo-EMFacility at
                      CSSB, supported by the UHH and DFG grantnumbers (INST
                      152/772-1|152/774-1|152/775-1|152/776-1|152/777-1 FUGG)},
      abstract     = {Successful sample preparation is the foundation to any
                      structural biology technique. Membrane proteins are of
                      particular interest as these are important targets for drug
                      design, but also notoriously difficult to work with. For
                      electron cryo-microscopy (cryo-EM), the biophysical
                      characterization of sample purity, homogeneity, and
                      integrity as well as biochemical activity is the
                      prerequisite for the preparation of good quality cryo-EM
                      grids as these factors impact the result of the
                      computational reconstruction. Here, we present a quality
                      control pipeline prior to single particle cryo-EM grid
                      preparation using a combination of biophysical techniques to
                      address the integrity, purity, and oligomeric states of
                      membrane proteins and its complexes to enable reproducible
                      conditions for sample vitrification. Differential scanning
                      fluorimetry following the intrinsic protein fluorescence
                      (nDSF) is used for optimizing buffer and detergent
                      conditions, whereas mass photometry and dynamic light
                      scattering are used to assess aggregation behavior,
                      reconstitution efficiency, and oligomerization. The data
                      collected on nDSF and mass photometry instruments can be
                      analyzed with web servers publicly available at
                      spc.embl-hamburg.de. Case studies to optimize conditions
                      prior to cryo-EM sample preparation of membrane proteins
                      present an example quality assessment to corroborate the
                      usefulness of our pipeline.},
      cin          = {CSSB-CF-PP / CSSB-LIV-KG / CSSB-CF-SPC / CSSB-CF-CRYO},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-CF-PP-20210530 /
                      I:(DE-H253)CSSB-LIV-KG-20220525 /
                      I:(DE-H253)CSSB-CF-SPC-20210520 /
                      I:(DE-H253)CSSB-CF-CRYO-20210520},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35813810},
      UT           = {WOS:000861787900001},
      doi          = {10.3389/fmolb.2022.882288},
      url          = {https://bib-pubdb1.desy.de/record/604257},
}