7MMN
Crystal Structure of the Prefusion RSV F Glycoprotein bound by human antibody AM14
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 | 2017-12-13 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 223.423, 183.002, 135.785 |
| Unit cell angles | 90.00, 103.14, 90.00 |
Refinement procedure
| Resolution | 42.330 - 3.570 |
| R-factor | 0.2035 |
| Rwork | 0.202 |
| R-free | 0.24530 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4mmu 4zyk |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.644 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.330 | 3.700 |
| High resolution limit [Å] | 3.570 | 3.570 |
| Rmerge | 0.200 | 0.890 |
| Rmeas | 0.250 | |
| Rpim | 0.130 | |
| Number of reflections | 62699 | 2848 |
| <I/σ(I)> | 8.3 | 1.74 |
| Completeness [%] | 88.2 | |
| Redundancy | 3.6 | |
| CC(1/2) | 0.960 | 0.510 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.2M NaCl, 0.1M MES pH 6.0, 20% w/v PEG 2000 MME |






