6SR8
Crystal structure of glutathione transferase Omega 2C from Trametes versicolor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-29 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979767 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 68.490, 141.960, 65.370 |
| Unit cell angles | 90.00, 116.21, 90.00 |
Refinement procedure
| Resolution | 22.147 - 1.940 |
| R-factor | 0.1985 |
| Rwork | 0.196 |
| R-free | 0.25260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6hjs |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.027 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 22.147 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.055 | 0.250 |
| Rmeas | 0.064 | 0.300 |
| Number of reflections | 42824 | 3095 |
| <I/σ(I)> | 13.33 | 5.28 |
| Completeness [%] | 97.1 | |
| Redundancy | 3.7 | |
| CC(1/2) | 1.000 | 0.960 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 277 | 20% (w/v) polyethylene glycol 4000, 10% (v/v) 2-Propanol and 0.1 M pH 7.5 HEPES |
