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@ARTICLE{Hermann:859976,
      author       = {Hermann, Johannes and Nowotny, Phillip and Schrader, Tobias
                      E. and Biggel, Philipp and Hekmat, Dariusch and
                      Weuster-Botz, Dirk},
      title        = {{N}eutron and {X}-ray crystal structures of {L}actobacillus
                      brevis alcohol dehydrogenase reveal new insights into
                      hydrogen-bonding pathways},
      journal      = {Acta crystallographica / F Structural biology
                      communications Section F},
      volume       = {74},
      number       = {12},
      issn         = {2053-230X},
      address      = {Oxford [u.a.]},
      publisher    = {Blackwell},
      reportid     = {FZJ-2019-00782},
      pages        = {754 - 764},
      year         = {2018},
      abstract     = {Lactobacillus brevis alcohol dehydrogenase (LbADH) is a
                      well studied homotetrameric enzyme which catalyzes the
                      enantioselective reduction of prochiral ketones to the
                      corresponding secondary alcohols. LbADH is stable and
                      enzymatically active at elevated temperatures and accepts a
                      broad range of substrates, making it a valuable tool in
                      industrial biocatalysis. Here, the expression, purification
                      and crystallization of LbADH to generate large, single
                      crystals with a volume of up to 1 mm3 suitable for neutron
                      diffraction studies are described. Neutron diffraction data
                      were collected from an H/D-exchanged LbADH crystal using the
                      BIODIFF instrument at the Heinz Maier-Leibnitz Zentrum
                      (MLZ), Garching, Germany to a resolution dmin of 2.15 Å
                      in 16 days. This allowed the first neutron crystal structure
                      of LbADH to be determined. The neutron structure revealed
                      new details of the hydrogen-bonding network originating from
                      the ion-binding site of LbADH and provided new insights into
                      the reasons why divalent magnesium (Mg2+) or manganese
                      (Mn2+) ions are necessary for its activity. X-ray
                      diffraction data were obtained from the same crystal at the
                      European Synchrotron Radiation Facility (ESRF), Grenoble,
                      France to a resolution dmin of 1.48 Å. The
                      high-resolution X-ray structure suggested partial occupancy
                      of Mn2+ and Mg2+ at the ion-binding site. This is supported
                      by the different binding affinity of Mn2+ and Mg2+ to the
                      tetrameric structure calculated via free-energy
                      molecular-dynamics simulations.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621) / 6G4 - Jülich Centre
                      for Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6215 /
                      G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30511668},
      UT           = {WOS:000452221700001},
      doi          = {10.1107/S2053230X18015273},
      url          = {https://juser.fz-juelich.de/record/859976},
}