6EB8
Crystal Structure of the Nipah Virus Phosphoprotein Multimerization Domain G519N
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-10-18 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 |
| Unit cell lengths | 48.001, 76.623, 80.538 |
| Unit cell angles | 100.46, 100.94, 108.05 |
Refinement procedure
| Resolution | 38.204 - 2.500 |
| R-factor | 0.2788 |
| Rwork | 0.276 |
| R-free | 0.33760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4n5b |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.277 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.204 | 2.600 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.310 | 2.010 |
| Rpim | 0.210 | 1.490 |
| Number of reflections | 35317 | 3976 |
| <I/σ(I)> | 4.1 | 0.7 |
| Completeness [%] | 98.6 | 98 |
| Redundancy | 3.7 | 3.8 |
| CC(1/2) | 0.970 | 0.100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | Protein at 12 mg/ml in 300mM NaCl and 10 mM Tris pH 8 mixed 1:1 with 10% (v/v) Glycerol, 5% (w/v) PEG 3000, 30% (v/v) PEG 400 and 0.1 M HEPES pH 7.5 |
