4B5C
Crystal structure of the peptidoglycan-associated lipoprotein from Burkholderia pseudomallei
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-11 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 101.940, 74.950, 72.920 |
| Unit cell angles | 90.00, 135.28, 90.00 |
Refinement procedure
| Resolution | 37.475 - 2.300 |
| R-factor | 0.2087 |
| Rwork | 0.206 |
| R-free | 0.24850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1oap |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.513 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.430 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.050 | 0.270 |
| Number of reflections | 16804 | |
| <I/σ(I)> | 13 | 3.5 |
| Completeness [%] | 96.8 | 95.7 |
| Redundancy | 2.2 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.3 | 30% PEG10K, 0.1M SODIUM ACETATE PH 5.3, 30% GLYCEROL FOR CRYOPROTECTION |
