1OE7
28kDa glutathione S-transferase from Schistosoma haematobium
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-10-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.427, 78.111, 53.502 |
| Unit cell angles | 90.00, 94.21, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| Rwork | 0.229 |
| R-free | 0.28900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gtb |
| RMSD bond length | 0.024 * |
| RMSD bond angle | 1.600 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.860 |
| High resolution limit [Å] | 1.810 | 1.810 |
| Rmerge | 0.071 | 0.220 |
| Number of reflections | 39246 | |
| <I/σ(I)> | 21.5 | 3.4 |
| Completeness [%] | 96.3 | 72 |
| Redundancy | 6.5 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 * | PROTEIN (~60MG/ML) WAS CRYSTALLIZED IN HANGING DROPS USING A WELL SOLUTION OF 2.1M AMMONIUM SULFATE, 100MM TRIS, PH7.2, 5MM BETA-MERCAPTOETHANOL, pH 8.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 2.1 (M) | |
| 2 | 1 | reservoir | Tris | 100 (mM) | pH7.2 |
| 3 | 1 | reservoir | beta-mercaptoethanol | 5 (mM) | |
| 4 | 1 | drop | protein | 66 (mg/ml) |
