Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals
Preliminary neutron diffraction analysis of challenging human manganese superoxide dismutase crystals
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DOI：
10.1107/s2053230x17003508
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发表时间：
2017-04-01
影响因子：
0.9
通讯作者：
Borgstahl, Gloria E. O.
中科院分区：
文献类型：
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作者：
Azadmanesh, Jahaun;Trickel, Scott R.;Borgstahl, Gloria E. O.
超氧化物歧化酶（SOD）是通过活性位点金属的循环还原和氧化将超氧化物歧化为氧和过氧化氢来保护免受氧化应激的酶。由于氢的位置数据有限，因此SOD的完整酶机制尚不清楚。本文介绍了橡树岭国家实验室利用全氘化和MaNDi光束线生长人锰SOD（MnSOD）大晶体和收集中子数据的方法。从其获得人类MnSOD数据集的晶体是具有最大晶胞边缘（240埃）的晶体，从该晶体已经通过中子衍射收集数据到足够的分辨率（2.30埃），其中可以观察到氢位置。
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.