2QOP
Crystal structure of the transcriptional regulator AcrR from Escherichia coli
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-10-15 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979249 |
Spacegroup name | P 2 2 21 |
Unit cell lengths | 48.218, 54.574, 73.726 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.550 |
Rwork | 0.228 |
R-free | 0.27300 |
Structure solution method | MAD |
RMSD bond length | 0.022 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SnB |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.640 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.076 | 0.306 |
Number of reflections | 6766 | |
<I/σ(I)> | 22 | 3.3 |
Completeness [%] | 98.2 | 85.2 |
Redundancy | 6.9 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 35% PEG 4000, 0.2M MgCl2, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |