7DWG
Crystal structure of a glutathione S-transferase mutant SbGSTU7(T53I) from Salix babylonica in complex with glutathione
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NFPSS BEAMLINE BL19U1 |
| Synchrotron site | NFPSS |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-12-01 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 55.148, 55.148, 184.164 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.340 - 1.670 |
| R-factor | 0.2083 |
| Rwork | 0.207 |
| R-free | 0.22470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7dwe |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.180 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.340 | 1.730 |
| High resolution limit [Å] | 1.670 | 1.670 |
| Number of reflections | 34121 | 3335 |
| <I/σ(I)> | 2.69 | |
| Completeness [%] | 99.8 | |
| Redundancy | 1 | |
| CC(1/2) | 1.000 | 1.000 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 289.15 | HEPES sodium, PEG 400, Ammonium sulfate |
