4W66
Crystal structure of Glutathione S-transferase domain protein from Haliangium ochraceum DSM 14365
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-13 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97924 |
| Spacegroup name | I 4 |
| Unit cell lengths | 130.400, 130.400, 70.147 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.950 - 2.360 |
| R-factor | 0.189 |
| Rwork | 0.186 |
| R-free | 0.23760 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.257 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0071) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.400 |
| High resolution limit [Å] | 2.360 | 6.400 | 2.360 |
| Rmerge | 0.132 | 0.049 | 0.986 |
| Rmeas | 0.133 | 0.054 | |
| Rpim | 0.058 | 0.021 | 0.467 |
| Total number of observations | 147328 | ||
| Number of reflections | 24250 | ||
| <I/σ(I)> | 7.3 | ||
| Completeness [%] | 99.9 | 99.1 | 100 |
| Redundancy | 6.1 | 6 | 5.3 |
| CC(1/2) | 0.993 | 0.772 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 0.2M Calcium Chloride, 0.1M This-Cl 20% PEG4000 |
