Crystallization and preliminary X-ray studies of hORF6, a novel human antioxidant enzyme

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Title
Crystallization and preliminary X-ray studies of hORF6, a novel human antioxidant enzyme
Author(s)
Hee Jeong Choi; S W Kang; C H Yang; S G Rhee; Seong Eon Ryu
Bibliographic Citation
Acta Crystallographica Section D-Biological Crystallography, vol. 54, pp. 436-437
Publication Year
1998
Abstract
HORF6 is a member of the novel antioxidant enzyme family found in humans. A recombinant form of hORF6 expressed and purified from E. coli has been crystallized by the hanging-drop method using various PEG's as precipitating agents. HORF6 crystallizes in two different monoclinic space groups, P21 and C2. The P21 crystals have unit-cell dimensions of a = 47.85, b = 75.17, c = 63.30 ? and β = 110.21°and contain two monomers per asymmetric unit, while the C2 crystals have unit-cell dimensions of a = 165.27, b = 95.44, c = 166.44 and 15 = 128.97°and contain more than six monomers per asymmetric unit. The P21 crystals with the smaller unit cell diffract X-rays better and behave well for the X-ray analysis. A native data set from a single crystal of the P21 space group has been collected to 2.0 ? resolution.
ISSN
0907-4449
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S0907444997011153
Type
Article
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1. Journal Articles > Journal Articles
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