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  • Title: Crystallization and preliminary X-ray studies of hORF6, a novel human antioxidant enzyme.
    Author: Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE.
    Journal: Acta Crystallogr D Biol Crystallogr; 1998 May 01; 54(Pt 3):436-7. PubMed ID: 9761920.
    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 A and beta = 110.21 degrees 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 A and beta = 128.97 degrees 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 gas been collected to 2.0 A resolution.
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