2VRN
The structure of the stress response protein DR1199 from Deinococcus radiodurans: a member of the DJ-1 superfamily
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-12-13 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 65.838, 88.562, 64.088 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.940 - 2.150 |
| R-factor | 0.203 |
| Rwork | 0.200 |
| R-free | 0.26100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gsi |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.313 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.270 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.080 | 0.520 |
| Number of reflections | 20998 | |
| <I/σ(I)> | 20.5 | 3 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 6.9 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.9 | 0.2 M MAGNESIUM FORMATE PH 5.9, 20% (W/V) PEG 3350 |
