8XC4
Nipah virus attachment glycoprotein head domain in complex with a broadly neutralizing antibody 1E5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL02U1 |
| Synchrotron site | SSRF |
| Beamline | BL02U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-09-13 |
| Detector | DECTRIS EIGER2 S 9M |
| Wavelength(s) | 0.9789 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 193.422, 193.422, 198.111 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.690 - 3.240 |
| R-factor | 0.219 |
| Rwork | 0.218 |
| R-free | 0.24680 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6vy5 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.109 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.18.2_3874: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.320 |
| High resolution limit [Å] | 3.240 | 3.240 |
| Rmerge | 0.189 | 0.189 |
| Number of reflections | 58116 | 58116 |
| <I/σ(I)> | 9.57 | |
| Completeness [%] | 97.1 | |
| Redundancy | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 1.5 M ammonium sulfate, 0.1 M sodium acetate trihydrate pH4.6 |






