4MF5
Crystal structure of glutathione transferase BgramDRAFT_1843 from Burkholderia graminis, Target EFI-507289, with traces of one GSH bound
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-08-16 |
| Detector | RAYONIX MX225HE |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 84.088, 84.088, 78.017 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.110 |
| R-factor | 0.11369 |
| Rwork | 0.113 |
| R-free | 0.12736 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ikh |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.517 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.130 |
| High resolution limit [Å] | 1.110 | 1.110 |
| Rmerge | 0.091 | |
| Number of reflections | 109376 | |
| <I/σ(I)> | 7.3 | 2.6 |
| Completeness [%] | 99.1 | 81.4 |
| Redundancy | 13.9 | 11.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | protein in 10 mM HEPES, pH 7.5, 150 mM sodium chloride, 5% glycerol, reservoir: 3.5 M sodium formate, pH 7.0, cryoprotectant: 20% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
