4XZA
The crystal structure of Erve virus nucleoprotein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-01-22 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.078, 104.286, 70.538 |
| Unit cell angles | 90.00, 92.38, 90.00 |
Refinement procedure
| Resolution | 46.038 - 1.800 |
| R-factor | 0.1694 |
| Rwork | 0.168 |
| R-free | 0.20220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3u3i |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.992 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 1.800 |
| Number of reflections | 61401 |
| <I/σ(I)> | 14.76 |
| Completeness [%] | 99.6 |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 1% Tryptone,0.05M HEPES,20% PEG 3350 |
