1OE8
28kDa glutathione S-transferase from Schistosoma haematobium (glutathione saturated)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-04-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.142, 77.705, 53.195 |
Unit cell angles | 90.00, 93.40, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.650 |
Rwork | 0.229 |
R-free | 0.28000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gtb |
RMSD bond length | 0.023 * |
RMSD bond angle | 1.300 * |
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 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.040 | 0.470 |
Number of reflections | 51735 | |
<I/σ(I)> | 40.9 | 2.7 |
Completeness [%] | 99.2 | 95 |
Redundancy | 4.1 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 * | PROTEIN (~60MG/ML) WITH 500UM EXCESS OF GSH 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) |