8JA5
Crystal structure of Nipah Virus attachment (G) glycoprotein in complex with neutralizing antibody 14F8
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 | 2021-10-20 |
| Detector | DECTRIS EIGER2 S 9M |
| Wavelength(s) | 0.9798 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 125.957, 125.957, 317.264 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.450 - 2.790 |
| R-factor | 0.218 |
| Rwork | 0.217 |
| R-free | 0.24490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6vy5 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.548 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.830 | 2.890 |
| High resolution limit [Å] | 2.790 | 2.790 |
| Rmerge | 0.104 | 0.104 |
| Number of reflections | 63808 | 63465 |
| <I/σ(I)> | 19.14 | |
| Completeness [%] | 98.9 | |
| Redundancy | 13.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 2.05M Ammonium sulfate, 10mM Barium chloride dihydrate, 0.1M Bis-Tris pH 5.5 |
