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@ARTICLE{Li:872853,
      author       = {Li, Long and Adachi, Motoyasu and Yu, Jian and Kato, Koji
                      and Shinoda, Akira and Ostermann, Andreas and Schrader,
                      Tobias E. and Ose, Toyoyuki and Yao, Min},
      title        = {{N}eutron crystallographic study of heterotrimeric
                      glutamine amidotransferase {CAB}},
      journal      = {Acta crystallographica / F Structural biology
                      communications Section F},
      volume       = {75},
      number       = {3},
      issn         = {2053-230X},
      address      = {Oxford [u.a.]},
      publisher    = {Blackwell},
      reportid     = {FZJ-2020-00321},
      pages        = {193 - 196},
      year         = {2019},
      abstract     = {Heterotrimeric glutamine amidotransferase CAB (GatCAB)
                      possesses anammonia-self-sufficient mechanism in which
                      ammonia is produced and usedin the inner complex by GatA and
                      GatB, respectively. The X-ray structure ofGatCAB revealed
                      that the two identified active sites of GatA and GatB
                      aremarkedly distant, but are connected in the complex by a
                      channel of 30 A ˚ inlength. In order to clarify whether
                      ammonia is transferred through this channelin GatCAB by
                      visualizing ammonia, neutron diffraction studies are
                      indispensable.Here, GatCAB crystals were grown to
                      approximate dimensions of2.8 0.8 0.8 mm (a volume of 1.8
                      mm3) with the aid of a polymer usingmicroseeding and
                      macroseeding processes. Monochromatic neutron
                      diffractiondata were collected using the neutron
                      single-crystal diffractometer BIODIFF atthe Heinz
                      Maier-Leibnitz Zentrum, Germany. The GatCAB crystals
                      belonged tospace group P212121, with unit-cell parameters a
                      = 74.6, b = 94.5, c = 182.5 A ˚ andwith one GatCAB complex
                      (molecular mass 119 kDa) in the asymmetric unit.This study
                      represented a challenge in current neutron diffraction
                      technology.},
      cin          = {JCNS-FRM-II / JCNS-1 / MLZ},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6215 /
                      G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30839294},
      UT           = {WOS:000460520900009},
      doi          = {10.1107/S2053230X19000220},
      url          = {https://juser.fz-juelich.de/record/872853},
}