3RRT
Structure of the RSV F protein in the post-fusion conformation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 200 |
| Detector technology | CCD |
| Collection date | 2011-02-10 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.024, 81.877, 271.948 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.170 - 3.200 |
| R-factor | 0.255 |
| Rwork | 0.253 |
| R-free | 0.28200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3rrr |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.090 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.260 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.208 | 0.470 |
| Number of reflections | 26109 | |
| <I/σ(I)> | 6.07 | 1.7 |
| Completeness [%] | 93.9 | 82.3 |
| Redundancy | 3.1 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.5 | 293 | 23% (w/v) PEG 3000, 0.1 M acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
