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 |