1AMO
THREE-DIMENSIONAL STRUCTURE OF NADPH-CYTOCHROME P450 REDUCTASE: PROTOTYPE FOR FMN-AND FAD-CONTAINING ENZYMES
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-04-17 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 103.280, 116.180, 119.770 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.600 |
| R-factor | 0.2 |
| Rwork | 0.200 |
| R-free | 0.31000 |
| Structure solution method | MIR |
| RMSD bond length | 0.007 |
| RMSD bond angle | 24.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.760 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.070 * | 0.308 * |
| Total number of observations | 171499 * | |
| Number of reflections | 41132 | |
| <I/σ(I)> | 13.5 | 2.4 |
| Completeness [%] | 91.5 | 85.8 |
| Redundancy | 4.2 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6.5 * | 19 * | drop solution was mixed with an equal volume of reservoir solution * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 25 (mg/ml) | |
| 2 | 1 | reservoir | PEG4500 | 21 (%) | |
| 3 | 1 | reservoir | HEPES | 150 (mM) | |
| 4 | 1 | reservoir | 5 (mM) | ||
| 5 | 1 | reservoir | 0.8 (M) |
