1PKZ
Crystal structure of human glutathione transferase (GST) A1-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-05-10 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9831 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 99.000, 89.888, 51.082 |
Unit cell angles | 90.00, 93.28, 90.00 |
Refinement procedure
Resolution | 65.940 - 2.100 |
R-factor | 0.1856 |
Rwork | 0.181 |
R-free | 0.22980 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.461 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 25470 | |
Completeness [%] | 96.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | MethylPEG2000, Tris-HCl, NaAc, 2-mercaptoethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |