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 |
