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Title: 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:
 [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:
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)
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 Volume: 73; Journal Issue: 4; Journal ID: ISSN 2053-230X
Publisher:
International Union of Crystallography
Country of Publication:
United States
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 States: 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 States. doi: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 States. doi: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 States},
year = {2017},
month = {3}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: 10.1107/S2053230X17003508

Citation Metrics:
Cited by: 10 works
Citation information provided by
Web of Science

Figures / Tables:

Figure 1 Figure 1: Fermentor growth of perdeuterated human MnSOD. SDS–PAGE of whole-cell lysate from cells grown in perdeuterated media immediately before and 13 h after induction. Monomeric human MnSOD has a molecular weight of 22 kDa. Samples were normalized to equivalent optical densities. Lane 1, molecular-mass markers (labelled in kDa). Lanemore » 2, pre-induction. Lane 3, post-induction.« less

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