5XNX
Crystallographic structure of the enzymatically active N-terminal domain of the Rel protein from Mycobacterium tuberculosis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-03-07 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | P 32 |
| Unit cell lengths | 161.710, 161.710, 75.560 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.020 - 3.700 |
| R-factor | 0.35105 |
| Rwork | 0.350 |
| R-free | 0.36765 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vj7 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.162 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.830 |
| High resolution limit [Å] | 3.700 | 3.700 |
| Rmerge | 0.050 | 0.243 |
| Number of reflections | 23372 | |
| <I/σ(I)> | 15.6 | 3.9 |
| Completeness [%] | 99.2 | 99.7 |
| Redundancy | 11.1 | 3.2 |
| CC(1/2) | 0.987 | 0.962 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 291 | 0.8M succinic acid, pH 7.0, 0.2M MgCl2, 0.2-0.4M Trimethylamin-N-oxide, 20% w/v Benzamidine hydrochloride hydrate |
