6SRA
Crystal structure of glutathione transferase Omega 2C from Trametes versicolor in complex with naringenin
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 | 2018-05-04 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97994 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 67.891, 141.959, 65.309 |
| Unit cell angles | 90.00, 115.70, 90.00 |
Refinement procedure
| Resolution | 34.369 - 2.206 |
| R-factor | 0.2249 |
| Rwork | 0.222 |
| R-free | 0.27620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6sr8 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.291 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.17) |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 37.430 | 37.430 | 2.270 |
| High resolution limit [Å] | 2.206 | 9.090 | 2.210 |
| Rmerge | 0.111 | 0.090 | 0.383 |
| Rmeas | 0.135 | 0.111 | 0.468 |
| Rpim | 0.076 | 0.063 | 0.266 |
| Total number of observations | 1125 | 6078 | |
| Number of reflections | 27025 | 395 | 2299 |
| <I/σ(I)> | 5.2 | 10.8 | 1.6 |
| Completeness [%] | 96.5 | 95.6 | 94 |
| Redundancy | 2.7 | 2.8 | 2.6 |
| CC(1/2) | 0.986 | 0.980 | 0.896 |
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 |
