8SIC
Crystal structure of Epstein-Barr virus glycoprotein 350 (gp350) in complex with Cy137C02, a monoclonal antibody isolated from macaques immunized with a gp350 nanoparticle vaccine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-11-18 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 2 21 |
| Unit cell lengths | 69.047, 71.377, 395.083 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 71.380 - 2.760 |
| R-factor | 0.248 |
| Rwork | 0.245 |
| R-free | 0.29490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | in-house structure of gp350 in a complex with a receptor fragment |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.659 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 71.430 | 2.910 |
| High resolution limit [Å] | 2.760 | 2.760 |
| Rmerge | 0.106 | 1.213 |
| Number of reflections | 51461 | 2338 |
| <I/σ(I)> | 15.5 | 2 |
| Completeness [%] | 99.9 | |
| Redundancy | 8.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | 18% PEG 8000, 0.22 M sodium acetate, 0.1 M sodium cacodylate pH 6.5 |
