1CL0
CRYSTAL STRUCTURE OF REDUCED THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 113 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-03-01 |
| Detector | RIGAKU |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 121.298, 121.298, 81.320 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 2.500 |
| Rwork | 0.200 |
| R-free | 0.29200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tde |
| RMSD bond length | 0.006 |
| RMSD bond angle | 25.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 2.650 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.119 * | |
| Number of reflections | 12009 | |
| <I/σ(I)> | 9.5 | 2.1 |
| Completeness [%] | 96.5 | 82.4 |
| Redundancy | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | 25 * | pH 8.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | 1,12-dodecanedioic acid | 19 (mM) | |
| 3 | 1 | reservoir | HEPES | 50 (mM) | |
| 4 | 1 | reservoir | ammonium sulfate | 200 (mM) | |
| 5 | 1 | reservoir | PEG3350 | 32-40 (%) |
