3Q74
Crystal Structure Analysis of the L7A Mutant of the Apo Form of Human Alpha Class Glutathione Transferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 113 |
| Detector technology | CCD |
| Collection date | 2009-10-05 |
| Detector | Bruker Platinum 135 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 99.345, 91.317, 51.374 |
| Unit cell angles | 90.00, 93.01, 90.00 |
Refinement procedure
| Resolution | 51.300 - 1.790 |
| R-factor | 0.2059 |
| Rwork | 0.203 |
| R-free | 0.27050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.902 |
| Data reduction software | SAINT |
| Data scaling software | SAINT (V7.34A) |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 51.300 | 3.873 | 1.862 |
| High resolution limit [Å] | 1.790 | 3.074 | 1.790 |
| Number of reflections | 42718 | ||
| <I/σ(I)> | 84.88 | ||
| Completeness [%] | 99.5 | ||
| Redundancy | 8.44 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop | 7.5 | 293 | 0.1 M Tris, 20% PEG 3350, 2 mM DTT, 0.02% azide, pH 7.5, hanging drop, temperature 293K |
