9MIK
Gallid alphaherpesvirus-1 large tegument protein bipartite NLS1 in complex with Importin alpha
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-10-13 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.95374 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 78.087, 89.924, 99.203 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.960 - 2.600 |
| R-factor | 0.1771 |
| Rwork | 0.175 |
| R-free | 0.21230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.554 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.960 | 2.720 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rpim | 0.038 | 0.216 |
| Number of reflections | 21815 | 2627 |
| <I/σ(I)> | 13.5 | |
| Completeness [%] | 99.0 | |
| Redundancy | 5.8 | |
| CC(1/2) | 0.997 | 0.864 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 296 | 0.6 M sodium citrate, 0.1 M HEPES |






