5LKW
Crystal structure of the peptidoglycan-associated lipoprotein (Pal) from Burkholderia cepacia in complex with DAP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-06-10 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.54 |
Spacegroup name | P 32 |
Unit cell lengths | 77.706, 77.706, 38.606 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 14.690 - 2.000 |
R-factor | 0.19138 |
Rwork | 0.188 |
R-free | 0.24909 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4b5c |
RMSD bond length | 0.021 |
RMSD bond angle | 1.847 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.084 | 0.438 |
Number of reflections | 16690 | |
<I/σ(I)> | 4.9 | 1.6 |
Completeness [%] | 100.0 | 82.3 |
Redundancy | 5.5 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 0.1M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3350, 10mM MgCl2 |