EC Number   |
|---|
    1.1.1.283 | crystal structures in an apo-form at 2.00 A and NADPH-complexed form at 2.40 A resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate |
| 1.1.1.283 | in complex with NADP, to 3.2 A resolution. Monoclinic space group P21, two Gre2 protomers per asymmetric unit |
| 1.1.1.283 | purified recombinant enzyme in apoform and in a complex with NADPH, X-ray diffraction structure determination and analysis at 2.0 A and 2.4 A, respectively |
| 1.1.1.283 | purified recombinant His-tagged enzyme Gre2 in apo-form and NADPH-complexed form, hanging drop vapor diffusion method, 24 mg/ml protein with or without 2 mM NADPH, with reservoir solution including 30% v/v glycerol, method, optimized, X-ray diffraction structure determination and analysis at resolutions of 2.8 and 3.02 A, respectively |
