3HTH
Crystal structure of multidrug binding protein EbrR complexed with proflavin
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 | 2008-07-28 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 99.719, 99.719, 133.730 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 86.390 - 2.700 |
R-factor | 0.2276 |
Rwork | 0.228 |
R-free | 0.27730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3hta |
RMSD bond length | 0.008 |
RMSD bond angle | 1.280 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 86.390 |
High resolution limit [Å] | 2.700 |
Rmerge | 0.064 |
Number of reflections | 21657 |
Redundancy | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 295 | 1.4 M Lithium sulfate, 0.1 M Tris-HCl, 0.01 M Nickel chloride, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |