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 |
