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 |