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  • 2000-2004  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 153-155 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Dihydropyrimidine dehydrogenase catalyzes the first and rate-limiting reaction in pyrimidine catabolism. The enzyme contains one FMN, one FAD and four Fe–S clusters per subunit of 1025 amino acids as prosthetic groups. It is also the major determinant of bioavailability and toxicity of 5-fluorouracil, a chemotherapeutic agent widely used in the treatment of solid tumors. Crystals of this enzyme diffracting to at least 2.5 Å have been obtained by the hanging-drop vapour-diffusion method and belong to space group P21 (unit-cell parameters a = 82.0, b = 159.3, c = 163.6 Å, β = 96.1°), with two homodimers per asymmetric unit.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature structural biology 8 (2001), S. 166-175 
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Many bacterial pathogens express lipooligosaccharides that mimic human cell surface glycoconjugates, enabling them to attach to host receptors and to evade the immune response. In Neisseria meningitidis, the galactosyltransferase LgtC catalyzes a key step in the biosynthesis of lipooligosaccharide ...
    Type of Medium: Electronic Resource
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  • 3
    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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