4L50
Crystal structures of the LsrR proteins complexed with phospho-AI-2 and its two different analogs reveal distinct mechanisms for ligand recognition
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-1A |
| Synchrotron site | Photon Factory |
| Beamline | BL-1A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-06-27 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.10000 |
| Spacegroup name | P 65 |
| Unit cell lengths | 116.809, 116.809, 79.975 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 34.520 - 2.100 |
| R-factor | 0.16902 |
| Rwork | 0.166 |
| R-free | 0.21806 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.983 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.520 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 33513 | |
| Completeness [%] | 97.3 | 92.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 293 | 5% PEG3350, 0.1 M Bis-Tris, 0.1 M NaCl, pH 6.5, VAPOR DIFFUSION, temperature 293K |
