8P24
The crystal structure of the C-terminal domain of Mengla nucleoprotein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALBA BEAMLINE XALOC |
| Synchrotron site | ALBA |
| Beamline | XALOC |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-05-12 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 56.748, 162.942, 175.363 |
| Unit cell angles | 90.00, 99.15, 90.00 |
Refinement procedure
| Resolution | 173.130 - 3.730 |
| R-factor | 0.2486 |
| Rwork | 0.248 |
| R-free | 0.26510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.668 |
| Data reduction software | autoPROC |
| Data scaling software | STARANISO |
| Phasing software | PHASER |
| Refinement software | REFMAC (dev_4788) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 173.130 | 4.270 |
| High resolution limit [Å] | 3.730 | 3.730 |
| Rmerge | 0.131 | 0.787 |
| Number of reflections | 8223 | 1356 |
| <I/σ(I)> | 4.7 | |
| Completeness [%] | 84.1 | |
| Redundancy | 3.6 | |
| CC(1/2) | 0.995 | 0.785 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.2M NaCl, 0.1M Cacodylate, 2M Ammonium Sulfate |
