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Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals
Author(s) -
Azadmanesh Jahaun,
Trickel Scott R.,
Weiss Kevin L.,
Coates Leighton,
Borgstahl Gloria E. O.
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17003508
Subject(s) - superoxide dismutase , manganese , hydrogen peroxide , crystal (programming language) , neutron diffraction , crystallography , chemistry , neutron , superoxide , materials science , enzyme , crystal structure , biochemistry , physics , computer science , organic chemistry , quantum mechanics , programming language
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.