% 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{Muderspach:434756,
      author       = {Muderspach, Sebastian J. and Tandrup, Tobias and Frandsen,
                      Kristian and Santoni, Gianluca and Poulsen, Jens-Christian
                      Navarro and Lo Leggio, Leila},
      title        = {{F}urther structural studies of the lytic polysaccharide
                      monooxygenase {A}o{AA}13 belonging to the starch-active
                      {AA}13 family},
      journal      = {Amylase},
      volume       = {3},
      number       = {1},
      issn         = {2450-9728},
      address      = {Warsaw, Poland},
      publisher    = {De Gruyter Open},
      reportid     = {PUBDB-2020-00310},
      pages        = {41 - 54},
      year         = {2019},
      abstract     = {Lytic polysaccharide monooxygenases (LPMOs) are recently
                      discovered copper enzymes that cleave recalcitrant
                      polysaccharides by oxidation. The structure of an
                      Aspergillus oryzae LPMO from the starch degrading family
                      AA13 (AoAA13) has previously been determined from an
                      orthorhombic crystal grown in the presence of copper, which
                      is photoreduced in the structure. Here we describe how
                      crystals reliably grown in presence of Zn can be Cu-loaded
                      post crystallization. A partly photoreduced structure was
                      obtained by severely limiting the X-ray dose, showing that
                      this LPMO is much more prone to photoreduction than others.
                      A serial synchrotron crystallography structure was also
                      obtained, showing that this technique may be promising for
                      further studies, to reduce even further photoreduction. We
                      additionally present a triclinic structure of AoAA13, which
                      has less occluded ligand binding site than the orthorhombic
                      one. The availability of the triclinic crystals prompted new
                      ligand binding studies, which lead us to the conclusion that
                      small starch analogues do not bind to AoAA13 to an
                      appreciable extent. A number of disordered conformations of
                      the metal binding histidine brace have been encountered in
                      this and other studies, and we have previously hypothesized
                      that this disorder may be a consequence of loss of copper.
                      We performed molecular dynamics in the absence of active
                      site metal, and showed that the dynamics in solution differ
                      somewhat from the disorder observed in the crystal, though
                      the extent is equally dramatic.},
      cin          = {DOOR ; HAS-User},
      ddc          = {570},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {6G3 - PETRA III (POF3-622) / BIOSTRUCT-X - Transnational
                      access and enhancement of integrated Biological Structure
                      determination at synchrotron X-ray radiation facilities
                      (283570)},
      pid          = {G:(DE-HGF)POF3-6G3 / G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1515/amylase-2019-0004},
      url          = {https://bib-pubdb1.desy.de/record/434756},
}