3LR3
Periplasmic domain of the risS sensor protein from Burkholderia pesuromallei, low pH native structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-09 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97650 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 58.883, 58.883, 75.973 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.460 - 2.100 |
| R-factor | 0.183 |
| Rwork | 0.181 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lr0 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.355 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.460 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.070 | 0.375 |
| Number of reflections | 9199 | |
| <I/σ(I)> | 13.2 | 3.25 |
| Completeness [%] | 98.5 | 87.1 |
| Redundancy | 13.7 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 289 | JCSG+ condition A6, 0.1 M phosphate-citrate pH 4.2, 0.2 M lithium sulfate, 25% PEG 1000, crystal tracking ID 208087a6, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
