5HR2
Crystal structure of thioredoxin L94A mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-11-30 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.9202 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 87.012, 47.917, 28.878 |
| Unit cell angles | 90.00, 101.95, 90.00 |
Refinement procedure
| Resolution | 28.252 - 1.200 |
| R-factor | 0.1329 |
| Rwork | 0.132 |
| R-free | 0.15150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1keb |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.122 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_2247) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.252 | 1.260 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.057 | 0.087 |
| Number of reflections | 34197 | |
| <I/σ(I)> | 11.9 | 6.3 |
| Completeness [%] | 94.3 | 81.3 |
| Redundancy | 3.3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | The drop was a 1:1 mix of protein (10 mg/ml in water) and reservoir solution (100 mM sodium acetate, 4 mM CuSO4, 18 % ethanol, pH 4.6) |
