4GJW
Structure of the tetramerization domain of Nipah virus phosphoprotein
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 | 2012-05-19 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.500, 85.600, 122.600 |
Unit cell angles | 90.00, 94.70, 90.00 |
Refinement procedure
Resolution | 48.750 - 3.000 |
R-factor | 0.178 |
Rwork | 0.175 |
R-free | 0.22900 |
Structure solution method | SAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.591 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | HKL2Map |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.750 | 3.080 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.143 | 0.653 |
Number of reflections | 47924 | |
<I/σ(I)> | 7.38 | 1.93 |
Completeness [%] | 99.5 | 99.9 |
Redundancy | 4.06 | 4.15 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5 | 293 | 17% PEG 3350, 1M LiCl, 0.1M sodium citrate, 0.1M Arginine, 4% Hexanediol, 0.001% NaN3, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |
1 | 5 | 293 | 17% PEG 3350, 1M LiCl, 0.1M sodium citrate, 0.1M Arginine, 4% Hexanediol, 0.001% NaN3, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |