3RRR
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 | 2010-12-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 113.170, 131.500, 164.280 |
| Unit cell angles | 90.00, 103.17, 90.00 |
Refinement procedure
| Resolution | 44.209 - 2.821 |
| R-factor | 0.2233 |
| Rwork | 0.221 |
| R-free | 0.26210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1g2c |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.856 |
| 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 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.159 | 0.353 |
| Number of reflections | 76177 | |
| <I/σ(I)> | 7.5 | 1.4 |
| Completeness [%] | 66.6 | 16.7 |
| Redundancy | 3.2 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 20% (w/v) PEG 3000, 0.1 M sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
