4N5B
Crystal structure of the Nipah virus phosphoprotein tetramerization domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-09 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 48.061, 76.877, 80.748 |
| Unit cell angles | 100.56, 100.85, 107.78 |
Refinement procedure
| Resolution | 46.369 - 2.200 |
| R-factor | 0.1895 |
| Rwork | 0.187 |
| R-free | 0.23820 |
| Structure solution method | AB INITIO PHASING |
| Starting model (for MR) | 4eij |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.635 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK |
| Phasing software | AMPLE |
| Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.370 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.063 | 0.298 |
| Number of reflections | 51813 | |
| <I/σ(I)> | 9.3 | 3 |
| Completeness [%] | 97.7 | 97.2 |
| Redundancy | 3.85 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295.5 | 0.1M imidazole pH 7.0, 25% PEG MME 550, 15% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 100K, temperature 295.5K |
