6EGU
Structure of RVFV envelope protein Gc in postfusion conformation in complex with 1,2-dipropionyl-sn-glycero-3-phosphocholine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-07-09 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.567, 195.729, 65.496 |
| Unit cell angles | 90.00, 113.96, 90.00 |
Refinement procedure
| Resolution | 37.883 - 2.300 |
| R-factor | 0.183 |
| Rwork | 0.180 |
| R-free | 0.23170 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hj1 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.757 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.150 | 2.360 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.175 | 0.689 |
| Rpim | 0.111 | 0.429 |
| Number of reflections | 65643 | |
| <I/σ(I)> | 9.3 | |
| Completeness [%] | 99.9 | |
| Redundancy | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 291 | 14.1% (w/v) PEG 5000 MME, 0.1 M Bis-Tris pH 6.2, 0.1M (NH4)2SO4, 1.8 mM UDM, and 5% glycerol. Note: 80 mM 1,2-dipropionyl-sn-glycero-3-phosphocholine added to protein solution |
