2VLI
Structure of Deinococcus radiodurans tunicamycin resistance protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-12-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9144, 0.9792 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 81.360, 118.160, 81.110 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.900 - 1.950 |
| R-factor | 0.176 |
| Rwork | 0.174 |
| R-free | 0.21400 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.580 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 22.930 | 1.970 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.090 | 0.520 |
| Number of reflections | 28689 | |
| <I/σ(I)> | 14.54 | 3 |
| Completeness [%] | 99.5 | 100 |
| Redundancy | 4.94 | 5.09 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 20 DEGREESC AFTER 3-6 DAYS USING HANGING DROPS CONTAINING 2 MICROL OF THE PROTEIN, 0.4-0.8 MICROL 0.1 M CDCL2 AND 1.6-1.2 MICROL OF A RESERVOIR SOLUTION CONTAINING 11-13% PEG 4000, 0.8 M SODIUM FORMATE AND 0.1 M SODIUM ACETATE PH 5.0 |
