5N2C
Crystal structure of the peptidoglycan-associated lipoprotein from Burkholderia cenocepacia
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 | 2015-12-20 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 70.433, 104.532, 110.436 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.958 - 1.800 |
| R-factor | 0.1798 |
| Rwork | 0.178 |
| R-free | 0.21870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4b5c |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.082 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.000 | 1.840 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.196 | 0.714 |
| Number of reflections | 38124 | 2222 |
| <I/σ(I)> | 9.1 | 3.4 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 8.9 | 9.2 |
| CC(1/2) | 0.998 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 10.5 | 293 | 2M NaH2PO4/ 0.8M KH2PO4; 0.1M CAPS pH 10.5; 0.2M LiSO4 |
