5FUS
Crystal structure of B. cenocepacia DfsA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 128.070, 128.070, 128.890 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.424 - 1.870 |
R-factor | 0.1678 |
Rwork | 0.166 |
R-free | 0.19770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3m6m |
RMSD bond length | 0.016 |
RMSD bond angle | 1.455 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.690 | 1.930 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.150 | 0.770 |
Number of reflections | 95772 | |
<I/σ(I)> | 6.7 | 1.8 |
Completeness [%] | 99.8 | 99.8 |
Redundancy | 5.2 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 50 MM TRIS-HCL 50 MM LISO4 50 MM NA2SO4 30% PEG 400 PH 8.5 |