6EGT
Structure of RVFV envelope protein Gc in postfusion conformation in complex with MES
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-09-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9801 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 72.306, 102.030, 198.892 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.497 - 2.500 |
| R-factor | 0.1971 |
| Rwork | 0.196 |
| R-free | 0.23510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hj1 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.920 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.3_1471) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.440 | 2.580 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.130 | 0.735 |
| Rpim | 0.080 | 0.541 |
| Number of reflections | 51348 | |
| <I/σ(I)> | 10 | |
| Completeness [%] | 99.5 | |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 291 | 12%(w/v) PEG 5000 MME, 0.1M MES 6.2, 0.1M (NH4)SO4, 1.8 mM UDM, 5% (v/v) glycerol |
