1E6B
Crystal structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX7.2 |
Synchrotron site | SRS |
Beamline | PX7.2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-10-17 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 75.164, 75.164, 140.520 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 1.650 |
R-factor | 0.196 * |
Rwork | 0.196 |
R-free | 0.23400 |
Structure solution method | SIRAS |
RMSD bond length | 0.011 |
RMSD bond angle | 1.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.690 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.040 | |
Number of reflections | 150341 | |
Completeness [%] | 94.7 | 95.9 |
Redundancy | 5-6 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 | 15 * | 11% PEG 8000, 0.2M MAGNESIUM ACETATE, 0.1 M SODIUM CACODYLA, pH 7.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | reservoir | PEG8000 | 11 (%(w/v)) | |
4 | 1 | reservoir | magnesium acetate | 0.2 (M) | |
5 | 1 | reservoir | sodium cacodylate | 0.1 (M) |