3HTA
Crystal structure of multidrug binding protein EbrR complexed with imidazole
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-09 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 76.471, 77.922, 203.265 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 67.700 - 2.300 |
R-factor | 0.2524 |
Rwork | 0.252 |
R-free | 0.29220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MODEL FORM MAD DATA OF EBRR |
RMSD bond length | 0.006 |
RMSD bond angle | 1.260 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 67.700 |
High resolution limit [Å] | 2.300 |
Rmerge | 0.030 |
Number of reflections | 54199 |
<I/σ(I)> | 48.3 |
Completeness [%] | 99.6 |
Redundancy | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 295 | 30% PEG 1000, 0.1 M Calcium chloride, 0.1 M Imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |