9LU3
LN1F9 Fab bound to Nipah Virus attachment (G) glycoprotein head domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL10U2 |
| Synchrotron site | SSRF |
| Beamline | BL10U2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-11-29 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 123.416, 125.155, 152.376 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.440 - 3.000 |
| R-factor | 0.2219 |
| Rwork | 0.219 |
| R-free | 0.26880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.326 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.600 | 3.100 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.128 | 0.594 |
| Number of reflections | 47546 | 4516 |
| <I/σ(I)> | 5.6 | 1.8 |
| Completeness [%] | 99.1 | |
| Redundancy | 5.2 | |
| CC(1/2) | 0.983 | 0.754 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 289 | 0.3 M ammonium formate, 0.1 M HEPES pH 7.0, 20 % [vol/vol] Sokalan CP5 |






