% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Schnherr:605882,
      author       = {Schönherr, Robert and Boger, Juliane and Lahey-Rudolph, J.
                      Mia and Harms, Mareike and Kaiser, Jacqueline and
                      Nachtschatt, Sophie and Wobbe, Marla and Duden, Rainer and
                      König, Peter and Bourenkov, Gleb and Schneider, Thomas R.
                      and Redecke, Lars},
      title        = {{A} streamlined approach to structure elucidation using in
                      cellulo crystallized recombinant proteins,
                      {I}n{C}ell{C}ryst},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-01564},
      pages        = {1709},
      year         = {2024},
      abstract     = {With the advent of serial X-ray crystallography on
                      microfocus beamlines at free-electron laser and synchrotron
                      facilities, the demand for protein microcrystals has
                      significantly risen in recent years. However, by in vitro
                      crystallization extensive efforts are usually required to
                      purify proteins and produce sufficiently homogeneous
                      microcrystals. Here, we present InCellCryst, an advanced
                      pipeline for producing homogeneous microcrystals directly
                      within living insect cells. Our baculovirus-based cloning
                      system enables the production of crystals from completely
                      native proteins as well as the screening of different
                      cellular compartments to maximize chances for protein
                      crystallization. By optimizing cloning procedures,
                      recombinant virus production, crystallization and crystal
                      detection, X-ray diffraction data can be collected 24 days
                      after the start of target gene cloning. Furthermore,
                      improved strategies for serial synchrotron diffraction data
                      collection directly from crystals within living cells
                      abolish the need to purify the recombinant protein or the
                      associated microcrystals.},
      cin          = {EMBL-User / EMBL / U Lübeck},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731 /
                      $I:(DE-H253)U_L__beck-20211012$},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101 / EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38402242},
      UT           = {WOS:001177163800012},
      doi          = {10.1038/s41467-024-45985-7},
      url          = {https://bib-pubdb1.desy.de/record/605882},
}