7NCU
Glutathione-S-transferase GliG mutant K127G in complex with oxidized glutathione
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-09-12 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 65 |
| Unit cell lengths | 126.260, 126.260, 64.890 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.500 |
| R-factor | 0.145 |
| Rwork | 0.143 |
| R-free | 0.17930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7nc3 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.367 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 1.600 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.055 | 0.615 |
| Number of reflections | 90330 | 16041 |
| <I/σ(I)> | 12.3 | 1.8 |
| Completeness [%] | 95.8 | |
| Redundancy | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 0.1 M tris pH 8.5, 29 % PEG6000 |
