3DD3
Crystal Structure of the Glutathione Transferase Pi enzyme in complex with the bifunctional inhibitor, Etharapta
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-08-18 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.77 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 76.690, 89.540, 68.990 |
| Unit cell angles | 90.00, 97.81, 90.00 |
Refinement procedure
| Resolution | 68.360 - 2.250 |
| R-factor | 0.2 |
| Rwork | 0.200 |
| R-free | 0.26000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5gss |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.606 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.21) |
| Phasing software | REFMAC (5.2.0019) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 68.360 | 2.370 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.100 | 0.560 |
| Total number of observations | 9208 | |
| Number of reflections | 21865 | |
| <I/σ(I)> | 4.3 | 1 |
| Completeness [%] | 99.5 | 96.6 |
| Redundancy | 3.6 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 100mM MES buffer pH 5.5 or 6.0, 22%(w/v) PEG 8000, 20mM CaCl2, 10mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
