% 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{Borshchevskiy:186014,
      author       = {Borshchevskiy, Valentin and Round, Ekaterina and Erofeev,
                      Ivan and Weik, Martin and Ishchenko, Andrii and Gushchin,
                      Ivan and Mishin, Alexey and Willbold, Dieter and Büldt,
                      Georg and Gordeliy, Valentin},
      title        = {{L}ow-dose {X}-ray radiation induces structural alterations
                      in proteins},
      journal      = {Acta crystallographica / D},
      volume       = {70},
      number       = {10},
      issn         = {1399-0047},
      address      = {Copenhagen},
      publisher    = {Munksgaard},
      reportid     = {FZJ-2015-00123},
      pages        = {2675 - 2685},
      year         = {2014},
      abstract     = {X-ray-radiation-induced alterations to protein structures
                      are still a severe problem in macromolecular
                      crystallography. One way to avoid the influence of radiation
                      damage is to reduce the X-ray dose absorbed by the crystal
                      during data collection. However, here it is demonstrated
                      using the example of the membrane protein bacteriorhodopsin
                      (bR) that even a low dose of less than 0.06 MGy may induce
                      structural alterations in proteins. This dose is about 500
                      times smaller than the experimental dose limit which should
                      ideally not be exceeded per data set (i.e. 30 MGy) and 20
                      times smaller than previously detected specific radiation
                      damage at the bR active site. To date, it is the lowest dose
                      at which radiation modification of a protein structure has
                      been described. Complementary use was made of
                      high-resolution X-ray crystallography and online
                      microspectrophotometry to quantitatively study low-dose
                      X-ray-induced changes. It is shown that structural changes
                      of the protein correlate with the spectroscopically observed
                      formation of the so-called bR orange species. Evidence is
                      provided for structural modifications taking place at the
                      protein active site that should be taken into account in
                      crystallographic studies which aim to elucidate the
                      molecular mechanisms of bR function.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000343060900017},
      pubmed       = {pmid:25286851},
      doi          = {10.1107/S1399004714017295},
      url          = {https://juser.fz-juelich.de/record/186014},
}