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Title 

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

Authors 

Hee Jeong ChoiS W KangC H YangS G RheeSeong Eon Ryu

Publisher 

International Union of Crystallography

Issue Date 

1998

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. 54, no. 0, pp. 436-437

Keywords 

antioxidantcrystallizationenzymeEscherichia coliX ray crystallographybacterial adhesionbacterial proteins

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.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, 54(0): 436-437

ISSN 

0907-4449

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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