8SGN
Crystal structure of Epstein-Barr virus glycoprotein 350 (gp350) in complex with Cy651H02, 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 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-02-25 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | H 3 |
| Unit cell lengths | 139.148, 139.148, 172.337 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.920 - 2.200 |
| R-factor | 0.1954 |
| Rwork | 0.193 |
| R-free | 0.23660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.644 |
| 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] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.150 | 0.368 |
| Number of reflections | 55717 | 1165 |
| <I/σ(I)> | 6.45 | 1.41 |
| Completeness [%] | 88.0 | 45.7 |
| Redundancy | 2.5 | 1.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | 1.72M ammonium sulfate, 0.1M Tris pH 8.0 |
