7NC6
Glutathione-S-transferase GliG in complex with cyclo[L-Phe-L-Ser]-bis-glutathione-adduct
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 | 2017-09-09 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.370, 85.300, 344.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.1859 |
| Rwork | 0.183 |
| R-free | 0.23810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7nc3 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 1.212 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.000 | 2.200 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.065 | 0.514 |
| Number of reflections | 92409 | 11933 |
| <I/σ(I)> | 11.5 | 2.5 |
| Completeness [%] | 99.0 | |
| Redundancy | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.2 M ammonium acetate, 0.1 M bis-tris pH 5.5, 25 % PEG3350 |
