3DGQ
Crystal structure of the glutathione transferase PI enzyme in complex with the bifunctional inhibitor, etharapta
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-11-20 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.930, 90.330, 68.960 |
| Unit cell angles | 90.00, 98.88, 90.00 |
Refinement procedure
| Resolution | 19.530 - 1.600 |
| R-factor | 0.196 |
| Rwork | 0.195 |
| R-free | 0.22700 |
| Starting model (for MR) | 5gss |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.539 |
| Data reduction software | d*TREK |
| Data scaling software | SCALA (3.2.21) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 19.530 | 19.530 | 1.690 |
| High resolution limit [Å] | 1.600 | 5.060 | 1.600 |
| Rmerge | 0.046 | 0.022 | 0.554 |
| Total number of observations | 7198 | 30550 | |
| Number of reflections | 61004 | ||
| <I/σ(I)> | 13.2 | 19 | 1.3 |
| Completeness [%] | 98.3 | 98.3 | 96.1 |
| Redundancy | 3.6 | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 100mM MES BUFFER PH 5.5, 22%(W/V) PEG 8000, 20mM CACL2, 10mM DTT, Small amounts of solid compound were streaked through the drops containing preformed crystals. These were soaked for 48hours., VAPOR DIFFUSION, HANGING DROP, temperature 298K |
