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@ARTICLE{Lee:417951,
      author       = {Lee, Dan Bi and Kim, Jong-Min and Seok, Jong Hyeon and Lee,
                      Ji-Hye and Jo, Jae Deok and Mun, Ji Young and Conrad,
                      Chelsie and Coe, Jesse and Nelson, Garrett and Hogue, Brenda
                      and White, Thomas A. and Zatsepin, Nadia and Weierstall, Uwe
                      and Barty, Anton and Chapman, Henry and Fromme, Petra and
                      Spence, John and Chung, Mi Sook and Oh, Chang-Hyun and Kim,
                      Kyung Hyun},
      title        = {{A}uthor {C}orrection: {S}upersaturation-controlled
                      microcrystallization and visualization analysis for serial
                      femtosecond crystallography},
      journal      = {Scientific reports},
      volume       = {8},
      number       = {1},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2019-00079},
      pages        = {6346},
      year         = {2018},
      abstract     = {Time-resolved serial femtosecond crystallography with X-ray
                      free electron laser (XFEL) holds the potential to view fast
                      reactions occurring at near-physiological temperature.
                      However, production and characterization of homogeneous
                      micron-sized protein crystals at high density remain a
                      bottleneck, due to the lack of the necessary equipments in
                      ordinary laboratories. We describe here
                      supersaturation-controlled microcrystallization and
                      visualization and analysis tools that can be easily used in
                      any laboratory. The microcrystallization conditions of the
                      influenza virus hemagglutinin were initially obtained with
                      low reproducibility, which was improved by employing a rapid
                      evaporation of hanging drops. Supersaturation-controlled
                      microcrystallization was then developed in a vapor diffusion
                      mode, where supersaturation was induced by evaporation in
                      hanging drops sequentially for durations ranging from
                      30 sec to 3 min, depending on the protein. It was
                      applied successfully to the microcrystal formation of
                      lysozyme, ferritin and hemagglutinin with high density.
                      Moreover, visualization and analysis tools were developed to
                      characterize the microcrystals observed by light microscopy.
                      The size and density distributions of microcrystals analyzed
                      by the tools were found to be consistent with the results of
                      manual analysis, further validated by high-resolution
                      microscopic analyses. Our supersaturation-controlled
                      microcrystallization and visualization and analysis tools
                      will provide universal access to successful XFEL studies.},
      cin          = {FS-CFEL-1},
      ddc          = {600},
      cid          = {I:(DE-H253)FS-CFEL-1-20120731},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29666410},
      UT           = {WOS:000430184400001},
      doi          = {10.1038/s41598-018-24178-5},
      url          = {https://bib-pubdb1.desy.de/record/417951},
}