5AE4
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 ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 107.472, 107.472, 297.771 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.570 - 3.300 |
R-factor | 0.1908 |
Rwork | 0.188 |
R-free | 0.24030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1utb |
RMSD bond length | 0.004 |
RMSD bond angle | 0.863 |
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] | 43.570 | 3.480 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.200 | 0.950 |
Number of reflections | 16127 | |
<I/σ(I)> | 10.9 | 2.6 |
Completeness [%] | 99.7 | 100 |
Redundancy | 5.5 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 0.2 M SODIUM TARTRATE, 0.2 M POTASSIUM THIOCYANATE 0.1 M TRIS-HCL PH 8.5, 20 % (W/V) PEG 8000 |