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@ARTICLE{Ohlin:276224,
      author       = {Ohlin, Mats and von Schantz, Laura and Schrader, Tobias E.
                      and Ostermann, Andreas and Logan, Derek T. and Fisher, S.
                      Zoë},
      title        = {{C}rystallization, neutron data collection, initial
                      structure refinement and analysis of a xyloglucan heptamer
                      bound to an engineered carbohydrate-binding module from
                      xylanase},
      journal      = {Acta crystallographica / F},
      volume       = {71},
      number       = {8},
      issn         = {2053-230X},
      address      = {Oxford [u.a.]},
      publisher    = {Blackwell},
      reportid     = {FZJ-2015-06689},
      pages        = {1072 - 1077},
      year         = {2015},
      abstract     = {Carbohydrate-binding modules (CBMs) are discrete parts of
                      carbohydrate-hydrolyzing enzymes that bind specific types of
                      carbohydrates. Ultra high-resolution X-ray crystallographic
                      studies of CBMs have helped to decipher the basis for
                      specificity in carbohydrate-protein interactions. However,
                      additional studies are needed to better understand which
                      structural determinants confer which carbohydrate-binding
                      properties. To address these issues, neutron
                      crystallographic studies were initiated on one
                      experimentally engineered CBM derived from a xylanase, X-2
                      L110F, a protein that is able to bind several different
                      plant carbohydrates such as xylan, [beta]-glucan and
                      xyloglucan. This protein evolved from a CBM present in
                      xylanase Xyn10A of Rhodothermus marinus. The protein was
                      complexed with a branched xyloglucan hepta­saccharide.
                      Large single crystals of hydrogenous protein (~1.6 mm3) were
                      grown at room temperature and subjected to H/D exchange.
                      Both neutron and X-ray diffraction data sets were collected
                      to 1.6 Å resolution. Joint neutron and X-ray refinement
                      using phenix.refine showed significant density for residues
                      involved in carbohydrate binding and revealed the details of
                      a hydrogen-bonded water network around the binding site.
                      This is the first report of a neutron structure of a CBM and
                      will add to the understanding of protein-carbohydrate
                      binding interactions.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; 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) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000359352700026},
      pubmed       = {pmid:26249702},
      doi          = {10.1107/S2053230X15011383},
      url          = {https://juser.fz-juelich.de/record/276224},
}