skip to main content


Title: Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals

Superoxide dismutases (SODs) are enzymes that protect against oxidative stress by dismutation of superoxide into oxygen and hydrogen peroxide through cyclic reduction and oxidation of the active-site metal. The complete enzymatic mechanisms of SODs are unknown since data on the positions of hydrogen are limited. Here, we present, methods for large crystal growth and neutron data collection of human manganese SOD (MnSOD) using perdeuteration and the MaNDi beamline at Oak Ridge National Laboratory. Furthermore, The crystal from which the human MnSOD data set was obtained is the crystal with the largest unit-cell edge (240 Å) from which data have been collectedvianeutron diffraction to sufficient resolution (2.30 Å) where hydrogen positions can be observed.
 [1] ;  [2] ; ORCiD logo [3] ; ORCiD logo [3] ;  [1]
  1. Nebraska Medical Center, Omaha, NE (United States). Eppley Inst. for Research in Cancer and Allied Diseases, Dept. of Biochemistry and Molecular Biology
  2. Nebraska Medical Center, Omaha, NE (United States). Eppley Inst. for Research in Cancer and Allied Diseases
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Biology and Soft Matter Division
Publication Date:
Grant/Contract Number:
AC05-00OR22725; 44-0307-1021-201; P30CA036727; 5P20RR016469
Published Article
Journal Name:
Acta Crystallographica. Section F, Structural Biology Communications
Additional Journal Information:
Journal Volume: 73; Journal Issue: 4; Journal ID: ISSN 2053-230X
International Union of Crystallography
Research Org:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); National Aeronautics and Space Administration (NASA); National Institutes of Health (NIH)
Country of Publication:
United States
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 60 APPLIED LIFE SCIENCES; manganese superoxide dismutase; neutron diffraction; perdeuteration; human; large unit cell
OSTI Identifier:
Alternate Identifier(s):
OSTI ID: 1407982