5DJL
Structure of WT Human Glutathione Transferase in complex with cisplatin in the presence of glutathione.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-11-09 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 77.450, 89.940, 68.780 |
Unit cell angles | 90.00, 98.03, 90.00 |
Refinement procedure
Resolution | 29.178 - 1.800 |
R-factor | 0.1507 |
Rwork | 0.149 |
R-free | 0.17750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5gss |
RMSD bond length | 0.004 |
RMSD bond angle | 0.955 |
Data reduction software | MOSFLM |
Data scaling software | Aimless (0.5.4) |
Phasing software | PHASER (2.5.3) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 31.580 | 31.580 | 1.840 |
High resolution limit [Å] | 1.800 | 9.000 | 1.800 |
Rmerge | 0.073 | 0.034 | 0.506 |
Rpim | 0.041 | 0.024 | 0.288 |
Total number of observations | 175670 | 1272 | 9899 |
Number of reflections | 43040 | ||
<I/σ(I)> | 9.6 | 17.6 | 2.9 |
Completeness [%] | 99.6 | 97.3 | 98.4 |
Redundancy | 4.1 | 3.5 | 4 |
CC(1/2) | 0.997 | 0.989 | 0.837 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 100MM MES, PH 5.5, PH 6.0, 28% (W/V) PEG 8000, 20MM CACL2 10MM DTT, 10MM GSH. Soaked in 0.1MM Cisplatin for 24hrs. |