Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals
Abstract
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 Å) from which data have been collected via neutron diffraction to sufficient resolution (2.30 Å) where hydrogen positions can be observed.
- Authors:
- Publication Date:
- Research Org.:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); National Aeronautics and Space Administration (NASA); National Institutes of Health (NIH)
- OSTI Identifier:
- 1437709
- Alternate Identifier(s):
- OSTI ID: 1407982
- Grant/Contract Number:
- AC05-00OR22725; 44-0307-1021-201; P30CA036727; 5P20RR016469
- Resource Type:
- Published Article
- Journal Name:
- Acta Crystallographica. Section F, Structural Biology Communications
- Additional Journal Information:
- Journal Name: Acta Crystallographica. Section F, Structural Biology Communications Journal Volume: 73 Journal Issue: 4; Journal ID: ISSN 2053-230X
- Publisher:
- International Union of Crystallography (IUCr)
- Country of Publication:
- United Kingdom
- Language:
- English
- Subject:
- 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 60 APPLIED LIFE SCIENCES; manganese superoxide dismutase; neutron diffraction; perdeuteration; human; large unit cell
Citation Formats
Azadmanesh, Jahaun, Trickel, Scott R., Weiss, Kevin L., Coates, Leighton, and Borgstahl, Gloria E. O. Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals. United Kingdom: N. p., 2017.
Web. doi:10.1107/S2053230X17003508.
Azadmanesh, Jahaun, Trickel, Scott R., Weiss, Kevin L., Coates, Leighton, & Borgstahl, Gloria E. O. Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals. United Kingdom. https://doi.org/10.1107/S2053230X17003508
Azadmanesh, Jahaun, Trickel, Scott R., Weiss, Kevin L., Coates, Leighton, and Borgstahl, Gloria E. O. Wed .
"Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals". United Kingdom. https://doi.org/10.1107/S2053230X17003508.
@article{osti_1437709,
title = {Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals},
author = {Azadmanesh, Jahaun and Trickel, Scott R. and Weiss, Kevin L. and Coates, Leighton and Borgstahl, Gloria E. O.},
abstractNote = {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 Å) from which data have been collected via neutron diffraction to sufficient resolution (2.30 Å) where hydrogen positions can be observed.},
doi = {10.1107/S2053230X17003508},
journal = {Acta Crystallographica. Section F, Structural Biology Communications},
number = 4,
volume = 73,
place = {United Kingdom},
year = {Wed Mar 29 00:00:00 EDT 2017},
month = {Wed Mar 29 00:00:00 EDT 2017}
}
https://doi.org/10.1107/S2053230X17003508
Web of Science
Figures / Tables:
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