1H6V
Mammalian thioredoxin reductase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 78.920, 140.464, 170.832 |
| Unit cell angles | 90.00, 94.64, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.000 |
| R-factor | 0.22555 |
| Rwork | 0.224 |
| R-free | 0.26295 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gra |
| RMSD bond length | 0.013 * |
| RMSD bond angle | 1.970 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.050 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.095 | 0.440 |
| Total number of observations | 212337 * | |
| Number of reflections | 69351 | |
| <I/σ(I)> | 11 | 7 |
| Completeness [%] | 92.7 | 77.6 |
| Redundancy | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | Zhong, L., (2000) Acta Crystallogr.,Sect.D, 56, 1191. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 60 (mg/ml) |
