1GWC
The structure of a tau class glutathione S-transferase from wheat, active in herbicide detoxification
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID13 |
| Synchrotron site | ESRF |
| Beamline | ID13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-04-15 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 87.982, 152.389, 146.772 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.250 |
| R-factor | 0.157 * |
| Rwork | 0.157 |
| R-free | 0.21100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1eem |
| RMSD bond length | 0.025 |
| RMSD bond angle | 2.260 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.000 | 2.300 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.119 | 0.350 |
| Number of reflections | 44559 | |
| <I/σ(I)> | 11 | 3 |
| Completeness [%] | 95.4 | 80 |
| Redundancy | 3 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | SITTING DROP METHOD WITH 1 MICROLITRE PROTEIN (10 MG/ML) AND 1 MICROLITRE WELL SOLUTION (1.1-1.5 M AMMONIUM SULPHATE, 0.2M LITHIUM SULPHATE 0.1M TRIS HCL PH 7.5 WITH 5MM S-HEXYLGLUTATHIONE) |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | pH7.5 |
| 3 | 1 | reservoir | ammonium sulfate | 1.1-1.5 (M) | |
| 4 | 1 | reservoir | lithium sulfate | 0.2 (M) | |
| 5 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH7.5 |
| 6 | 1 | reservoir | S-hexylglutathione | 5 (mM) |
