8FUA
Crystal structure of mouse Importin alpha in complex with Hendra virus matrix protein NLS1
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 | 2019-07-25 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 78.488, 89.859, 99.829 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.420 - 1.900 |
| R-factor | 0.1737 |
| Rwork | 0.173 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6bw0 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.178 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (1.14_3260) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.420 | 1.940 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.085 | 1.376 |
| Rpim | 0.050 | 0.820 |
| Number of reflections | 56224 | 26486 |
| <I/σ(I)> | 11.9 | |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 7.2 | 7.1 |
| CC(1/2) | 0.998 | 0.602 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.1M sodium HEPES, 0.72M sodium citrate, 1% dithiothreitol |
