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Literature summary for 1.6.5.2 extracted from

  • Faig, M.; Bianchet, M.A.; Talalay, P.; Chen, S.; Winski, S.; Ross, D.; Amzel, L.M.
    Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release (2000), Proc. Natl. Acad. Sci. USA, 97, 3177-3182.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion from a solution containing 10-15 mg/ml enzyme in 25 mM Tris-HCl, pH 8.0, 0.005 mM FAD, mixed with equal volumes of reservoir solution consisting of 30% polyethylene glycol 3350, 200 mM sodium acetate and 100 mM sodium tricine, pH 8.5, x-ray structure, 1.7 A resolution Homo sapiens
hanging drop vapor diffusion from a solution containing 10-15 mg/ml enzyme in 25 mM Tris-HCl, pH 8.0, 0.005 mM FAD, mixed with equal volumes of reservoir solution consisting of 30% polyethylene glycol 3350, 200 mM sodium acetate and 100 mM sodium tricine, pH 8.5, X-ray structure, 2.8 A resolution Mus musculus

Organism

Organism UniProt Comment Textmining
Homo sapiens P15559
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Mus musculus Q64669
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