5AE5
Structures of inactive and activated DntR provide conclusive evidence for the mechanism of action of LysR transcription factors
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 107.132, 107.132, 297.844 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.142 - 2.645 |
R-factor | 0.2009 |
Rwork | 0.199 |
R-free | 0.22720 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1utb |
RMSD bond length | 0.004 |
RMSD bond angle | 0.969 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.140 | 2.790 |
High resolution limit [Å] | 2.640 | 2.640 |
Rmerge | 0.100 | 1.000 |
Number of reflections | 30522 | |
<I/σ(I)> | 13.5 | 2.1 |
Completeness [%] | 97.7 | 98.1 |
Redundancy | 7.9 | 8.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 0.2 M SODIUM POTASSIUM TARTRATE, 0.1 M TRIS-HCL PH 8.0, 5 % (W/V) PEG 6000 |