EC Number   |
|---|
    1.3.1.24 | - |
| 1.3.1.24 | an X-ray diffraction experiment using a native BVR crystal is performed on the BL38B1 beamline. The crystal belongs to the orthorhombic space group P2-1-2-1-2-1, with unit-cell parameters a = 58.8, b = 88.4, c = 132.6 A. A complete data set is collected to a resolution of 2.34 A |
| 1.3.1.24 | apo enzyme and in complex with NADH |
| 1.3.1.24 | apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50 mM Tris-HCl (pH 7.25), 0.2 M sodium acetate and 0.2 mM Cymal-2 |
| 1.3.1.24 | apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50mM Tris-HCl (pH 7.25), 0.2M sodium acetate and 0.2mM Cymal-2 |
| 1.3.1.24 | BVR-NADH complex, NH2-terminal domain in dinucleotide binding |
| 1.3.1.24 | crystals of the biliverdin reductase obtained by sitting-drop vapour-diffusion method, enzyme diffraction data collected to 1.6 A, crystals belong to the orthorhombic space group P212121 with unit-cell parameters a=58.89, b=70.41, c=87.76 A |
| 1.3.1.24 | hanging drop vapor diffusion method, using 27% (w/v) PEG 3350, 0.2M MgCl2 and 0.1 M BisTris at pH 5.5 |
