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 |