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Title
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Crystallization and preliminary X-ray diffraction studies of human cytochrome P450 reductase.
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Authors
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Q.Zhao,
G.Smith,
S.Modi,
M.Paine,
R.C.Wolf,
D.Tew,
L.Y.Lian,
W.U.Primrose,
G.C.Roberts,
H.P.Driessen.
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Ref.
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J Struct Biol, 1996,
116,
320-325.
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PubMed id
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Abstract
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The two functional domains of a cloned human fibroblast NADPH-cytochrome P450
reductase have been expressed in Escherichia coli and purified on the milligram
scale for crystallization studies. One domain contains the cofactor FMN-binding
site and the other contains the binding sites for cofactor FAD and substrate
NADPH. Crystals of both domains have been obtained by the microbatch method. The
crystals of the FMN domain belong to the monoclinic space group P21, with unit
cell dimensions of a = 39.3 A, b = 51.5 A, c = 47.8 A, and beta = 105.7 degrees
and have one molecule in the asymmetric unit. Diffraction data up to 2.3 A were
collected with a merging residual on intensity of 9.3%. The crystals of the
FAD/NADPH domain belong to the ortho-rhombic space group P212121 with unit cell
dimensions of a = 55.9 A, b = 58.6 A, c = 131.1 A and have one molecule in the
asymmetric unit. Diffraction data up to 2.6 A were collected with a merging
residual on intensity of 8.0%.
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