4GF0
Crystal structure of glutahtione transferase homolog from sulfitobacter, TARGET EFI-501084, with bound glutathione
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-07-20 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 95.844, 95.844, 94.911 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.913 - 1.750 |
| R-factor | 0.1661 |
| Rwork | 0.165 |
| R-free | 0.19340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gdr |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.089 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 31.948 | 31.948 | 1.840 |
| High resolution limit [Å] | 1.750 | 5.530 | 1.750 |
| Rmerge | 0.120 | 0.040 | 0.799 |
| Total number of observations | 19300 | 88398 | |
| Number of reflections | 45143 | ||
| <I/σ(I)> | 14.3 | 16.5 | 1 |
| Completeness [%] | 99.9 | 96.1 | 100 |
| Redundancy | 13.9 | 12.5 | 13.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 298 | 0.2 M Lithium Sulfate, 0.1 mM Bis-Tris pH 6.5, 25% PEG3350, sitting drop vapor diffusion, temperature 298K |
