9T1M
Nuclear export protein/Non-structural protein 2 (NEP/NS2) in complex with artificial alpha Rep protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-04-30 |
| Detector | DECTRIS EIGER2 X 9M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 136.809, 136.809, 71.362 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 68.400 - 2.330 |
| R-factor | 0.2188 |
| Rwork | 0.217 |
| R-free | 0.24890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.402 |
| Data reduction software | DIALS |
| Data scaling software | STARANISO |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.21.2_5419+SVN) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 68.420 | 2.840 |
| High resolution limit [Å] | 2.330 | 2.620 |
| Rmerge | 0.190 | 1.000 |
| Rpim | 0.060 | 0.440 |
| Number of reflections | 25648 | 924 |
| <I/σ(I)> | 11.2 | 1.4 |
| Completeness [%] | 94.4 | 61.2 |
| Redundancy | 10.7 | 5.7 |
| CC(1/2) | 0.960 | 0.960 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 293 | 13 mg.mL-1 protein consisting of 1:1 molar ratio NEP and alpha-Rep E4 0.2 M sodium acetate pH 5.0, 12-16 % PEG 6K, 0.2 M CaCl2 |
