7Y55
Crystal structure of a glutathione S-transferase Tau1 from Pinus densata in complex with GSH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-05-14 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 166.402, 55.509, 119.754 |
| Unit cell angles | 90.00, 112.50, 90.00 |
Refinement procedure
| Resolution | 38.434 - 2.191 |
| R-factor | 0.276769379248 |
| Rwork | 0.276 |
| R-free | 0.30209 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4top |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.235 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692+SVN) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 10.000 | 2.230 |
| High resolution limit [Å] | 2.190 | 5.940 | 2.190 |
| Rmerge | 0.167 | 0.151 | 0.703 |
| Rmeas | 0.182 | 0.165 | 0.811 |
| Rpim | 0.073 | 0.065 | 0.389 |
| Total number of observations | 275021 | ||
| Number of reflections | 49207 | 2718 | 1717 |
| <I/σ(I)> | 3.3 | ||
| Completeness [%] | 94.5 | 99.7 | 66.6 |
| Redundancy | 5.6 | 6.3 | 3.3 |
| CC(1/2) | 0.968 | 0.742 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 289 | 0.1 M MES monohydrate pH 5.5, 25% v/v Polyethylene glycol 400 |
