1LC0
Structure of Biliverdin Reductase and the Enzyme-NADH Complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-05-01 |
Detector | MARRESEARCH |
Wavelength(s) | 0.98 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.780, 75.730, 76.080 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.000 * - 1.200 |
Rwork | 0.222 |
R-free | 0.23200 * |
Structure solution method | MIR |
RMSD bond length | 0.006 |
RMSD bond angle | 23.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.000 * | 1.210 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.048 * | 0.450 * |
Total number of observations | 636022 * | |
Number of reflections | 95268 * | |
Completeness [%] | 98.1 | 99.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 10.5 | 4 * | 2.0 M Na+/K+ phosphate, 100 mM CAPS, 200 mM lithium sulfate (Emerald Screen Wizard-I condition 27), pH 10.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6.5 (mg/ml) | |
2 | 1 | reservoir | sodium potassium phosphate | 2.0 (M) | |
3 | 1 | reservoir | CAPS | 100 (mM) | pH10.5 |
4 | 1 | reservoir | lithium sulfate | 200 (mM) |