期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 73, 期 -, 页码 235-240出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X17003508
关键词
manganese superoxide dismutase; neutron diffraction; perdeuteration; human; large unit cell
资金
- National Aeronautics and Space Administration [44-0307-1021-201]
- National Institutes of Health [P30CA036727]
- National Institutes of Health, National Center for Research Resources [5P20RR016469]
- National Institutes of Health, National Institute of General Medical Sciences [8P20GM103427]
- U.S. Department of Energy
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, methods are presented for large crystal growth and neutron data collection of human manganese SOD (MnSOD) using perdeuteration and the MaNDi beamline at Oak Ridge National Laboratory. The crystal from which the human MnSOD data set was obtained is the crystal with the largest unit-cell edge (240 angstrom) from which data have been collected via neutron diffraction to sufficient resolution (2.30 angstrom) where hydrogen positions can be observed.
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