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@INPROCEEDINGS{Schrader:1053145,
      author       = {Schrader, Tobias Erich and Ostermann},
      title        = {{WHAT} {NEUTRONS} {CAN} {DO} {FOR} {YOU}:{THE} {SINGLE}
                      {CRYSTAL} {NEUTRON} {DIFFRACTOMETER} {BIODIFF} {AT} {THE}
                      {HEINZ} {MAIER}-{LEIBNITZ} {ZENTRUM}},
      reportid     = {FZJ-2026-01477},
      year         = {2025},
      abstract     = {Neutrons are scattered from the nuclei and x-rays are
                      scattered from the electrons of the atoms in a protein
                      crystal. This renders these two scattering probes as being
                      complementary to each other. The neutrons can see the
                      hydrogen atom positions in a protein crystal. This allows to
                      determine protonation states of crucial amino acid residues
                      in the active centre of an enzyme or one can detect water
                      clusters and proton paths to the active centre by locating
                      water molecules and their exact orientation and hydrogen
                      bonding. In this contribution neutron protein
                      crystallography is introduced using the example of alcohol
                      dehydrogenase from the organism Lactobacillus brevis
                      (LbADH), an enzyme which catalyzes the reduction of
                      prochiral ketones to the corresponding secondary alcohols
                      [1]. The data set for this project was taken with the
                      instrument BIODIFF. The neutron single crystal
                      diffractometer BIODIFF at the research reactor Heinz
                      Maier-Leibnitz (FRM II) is especially designed to collect
                      data from crystals with large unit cells. The main field of
                      application is the structural analysis of proteins,
                      especially the determination of hydrogen atom positions.
                      BIODIFF is a joint project of the Jülich Centre for Neutron
                      Science (JCNS) and the FRM II. BIODIFF is designed as a
                      monochromatic instrument with a narrow wavelength spread of
                      less than 3 $\%.$ To cover a large solid angle the main
                      detector of BIODIFF consists of a neutron imaging plate in a
                      cylindrical geometry with online read-out capability. The
                      resulting data led to a better understanding of the role of
                      the Magnesium ion in substrate binding and it showed a new
                      hydrogen bonding network close to the active centre of the
                      enzyme. It also showed nicely the complementary nature of
                      x-ray and neutron protein crystallography. The metal ion in
                      Figure 1 has not been detected by neutron scattering but it
                      was easily seen by x-ray scattering. The reason for this
                      lies in a cancellation effect between the negative
                      scattering length of Manganese ions and the average positive
                      scattering lengths of Magnesium ions which just cancel to
                      zero in this position. The Magnesium ions were present in
                      the crystallization condition, but the Manganese Ions must
                      stem from the expression of the protein in the E.coli
                      expression system.},
      month         = {Oct},
      date          = {2025-10-20},
      organization  = {Enzyme Engineering Conference,
                       Helsingor (Denmark), 20 Oct 2025 - 24
                       Oct 2025},
      subtyp        = {After Call},
      cin          = {JCNS-FRM-II / MLZ / JCNS-4},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-4-20201012},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)24},
      url          = {https://juser.fz-juelich.de/record/1053145},
}