7PNO
C terminal domain of Nipah Virus Phosphoprotein fused to the Ntail alpha more of the Nucleoprotein.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-09-09 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9394 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 60.460, 131.970, 156.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 23.940 - 2.790 |
| R-factor | 0.20548 |
| Rwork | 0.203 |
| R-free | 0.25743 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.561 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | AMPLE |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 78.450 | 2.980 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.070 | 0.349 |
| Number of reflections | 16111 | 2844 |
| <I/σ(I)> | 17.1 | |
| Completeness [%] | 99.8 | |
| Redundancy | 8.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 293 | 20% PEG 550, Sodium acetate 100 mM pH 4 |
