5LKD
Crystal structure of the Xi glutathione transferase ECM4 from Saccharomyces cerevisiae in complex with glutathione
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 | P 1 21 1 |
| Unit cell lengths | 55.440, 82.440, 80.580 |
| Unit cell angles | 90.00, 95.31, 90.00 |
Refinement procedure
| Resolution | 47.582 - 1.680 |
| R-factor | 0.161 |
| Rwork | 0.159 |
| R-free | 0.20030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ppu |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.456 |
| 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] | 47.590 | 1.720 |
| High resolution limit [Å] | 1.680 | 1.680 |
| Rmerge | 0.055 | |
| Number of reflections | 78066 | |
| <I/σ(I)> | 17.9 | 1.9 |
| Completeness [%] | 95.0 | 74.3 |
| Redundancy | 3.8 | 3.7 |
| CC(1/2) | 0.990 | 0.760 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 277 | 20% (w/v) PEG 2000 MME, 0.1 M Tris pH 7.0 |
