4LVQ
Crystal structure of the M. tuberculosis phosphate binding protein PstS3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-05-25 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97625 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 36.207, 229.253, 39.103 |
| Unit cell angles | 90.00, 100.03, 90.00 |
Refinement procedure
| Resolution | 38.505 - 2.300 |
| R-factor | 0.2389 |
| Rwork | 0.236 |
| R-free | 0.27540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.561 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 2.640 |
| High resolution limit [Å] | 2.300 | 2.640 | 2.300 |
| Rmerge | 0.170 | 0.270 | |
| Number of reflections | 26706 | ||
| <I/σ(I)> | 7.3 | 4.8 | |
| Completeness [%] | 97.4 | 97.5 | 96.5 |
| Redundancy | 3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1 M MES monohydrate, pH 6.5, 12% w/v PEG 20000, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
