6QHG
Structure of the cap-binding domain of Rift Valley Fever virus L protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
| Synchrotron site | PETRA III, EMBL c/o DESY |
| Beamline | P13 (MX1) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-09-24 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 31.580, 53.681, 135.987 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.133 - 1.483 |
| R-factor | 0.1539 |
| Rwork | 0.152 |
| R-free | 0.19350 |
| Structure solution method | SAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.904 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | AutoSol |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 67.990 | 1.536 |
| High resolution limit [Å] | 1.483 | 1.483 |
| Rmerge | 0.113 | 0.403 |
| Rmeas | 0.123 | 0.437 |
| Rpim | 0.048 | 0.168 |
| Number of reflections | 39006 | |
| <I/σ(I)> | 10 | |
| Completeness [%] | 99.0 | |
| Redundancy | 12 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 24% PEG 2000 MME, 200 mM Trimethylamine N-oxide, 2 mM TCEP, 5 mM dithiothreitol, 2 mM m7GTP and 100 mM Tris, pH 8.5 |






