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    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1191-1193 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Mammalian cytosolic thioredoxin reductase is a homodimer of 55 kDa subunit containing an essential penultimate selenocysteine residue. An active analogue of the rat enzyme in which cysteine replaces selenocysteine has been expressed in Escherichia coli cells at high levels and purified to homogeneity. The pure enzyme contains one FAD per subunit and shows spectral properties identical to that of the wild-type thioredoxin reductase. The isolated enzyme in its oxidized and reduced forms or the enzyme complexed with NADP+ was crystallized by the hanging-drop vapour-diffusion method. The diffraction pattern extends to 3 Å resolution. The crystals are monoclinic, space group P21, with unit-cell parameters a = 78.9, b = 140.5, c = 170.8 Å, α = 94.6°. There are three dimeric molecules in the asymmetric unit.
    Type of Medium: Electronic Resource
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