3MAK
Crystal structure of Glutathione transferase dmGSTD1 from Drosophila melanogaster, in complex with glutathione
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-27 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 71.352, 63.137, 54.240 |
| Unit cell angles | 90.00, 129.55, 90.00 |
Refinement procedure
| Resolution | 18.260 - 1.800 |
| R-factor | 0.162 |
| Rwork | 0.160 |
| R-free | 0.20000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3f6f |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.213 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 3.870 | 1.800 |
| Rmerge | 0.029 | 0.026 | 0.040 |
| Number of reflections | 16992 | ||
| <I/σ(I)> | 47.9 | ||
| Completeness [%] | 97.6 | 88 | 94.4 |
| Redundancy | 3.5 | 3.2 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 0.1M Tris pH 8.5, 25% (w/v) PEG 4000, 0.2M Lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
