ArticleActa crystallographica. Section F, Structural biology communications2017
Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- The curious life of human mitochondrial SOD2.International journal of biological macromolecules · 2026Review
- The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase.Nature communications · 2025Article
- Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.Nature communications · 2024Article
- The role of Tyr34 in proton-coupled electron transfer of human manganese superoxide dismutase.Research square · 2024Article
- Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.Research square · 2024Article
- Perfect Crystals: microgravity capillary counterdiffusion crystallization of human manganese superoxide dismutase for neutron crystallography.NPJ microgravity · 2023Article
- Cryotrapping peroxide in the active site of human mitochondrial manganese superoxide dismutase crystals for neutron diffraction.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase.Nature communications · 2021Article
- Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Improving the accuracy and resolution of neutron crystallographic data by three-dimensional profile fitting of Bragg peaks in reciprocal space.Acta crystallographica. Section D, Structural biology · 2018Article
- Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction.Acta crystallographica. Section F, Structural biology communications · 2018Article
- A Review of the Catalytic Mechanism of Human Manganese Superoxide Dismutase.Antioxidants (Basel, Switzerland) · 2018Review
- Ewald: an extended wide-angle Laue diffractometer for the second target station of the Spallation Neutron Source.Journal of applied crystallography · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
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.
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