1BED
STRUCTURE OF DISULFIDE OXIDOREDUCTASE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 290 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-08-17 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 64.000, 91.500, 64.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.205 |
| Rwork | 0.205 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dsb |
| RMSD bond length | 0.007 |
| RMSD bond angle | 23.100 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.062 | 0.341 |
| Total number of observations | 60945 * | |
| Number of reflections | 12974 | |
| <I/σ(I)> | 13.1 | 3.4 |
| Completeness [%] | 98.2 | 91.7 |
| Redundancy | 5.7 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.8 * | 20 * | 10-13% EG 4K, 0.1M MES, PH 6.0-6.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 23 (mg/ml) | |
| 2 | 1 | drop | 40 (mM) | ||
| 3 | 1 | drop | HEPES | 10 (mM) | |
| 4 | 1 | drop | EDTA | 0.5 (mM) | |
| 5 | 1 | reservoir | PEG4000 | 10-13 (%) | |
| 6 | 1 | reservoir | MES | 0.1 (M) |
