3H4K
Crystal structure of the wild type Thioredoxin glutatione reductase from Schistosoma mansoni in complex with auranofin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-06-12 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.98 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 147.515, 102.166, 60.572 |
| Unit cell angles | 90.00, 114.16, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.550 |
| R-factor | 0.23145 |
| Rwork | 0.230 |
| R-free | 0.25630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v6o |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.913 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.590 |
| High resolution limit [Å] | 2.550 | 2.550 |
| Rmerge | 0.120 | 0.480 |
| Number of reflections | 26954 | |
| <I/σ(I)> | 14.7 | 2.4 |
| Completeness [%] | 99.7 | |
| Redundancy | 5.2 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | Hepes pH 7.0, 20% PEG3350, 0.1M KI, 5mM GSH, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
