Crystallization and preliminary X-ray studies of hORF6, a novel human antioxidant enzyme.
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.
Choi
H J
HJ
Division of Protein Engineering, Korea Research Institute of Bioscience and Biotechnology, KIST, PO Box 115, Yusong, Taejon 305-600, South Korea.
Kang
S W
SW
Yang
C H
CH
Rhee
S G
SG
Ryu
S E
SE
D000975:Antioxidants / Q000737:chemistry*; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D004926:Escherichia coli; D006801:Humans; D010544:Peroxidases / Q000737:chemistry*; D054464:Peroxiredoxins; D011994:Recombinant Proteins / Q000096:biosynthesis; D014961:X-Ray Diffraction
D000975:Antioxidants; D001426:Bacterial Proteins; D011994:Recombinant Proteins; D010544:Peroxidases; D054464:Peroxiredoxins