2R7J
Crystal Structure of rotavirus non structural protein NSP2 with H225A mutation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9793990 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 106.963, 106.963, 151.147 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.600 |
Rwork | 0.226 |
R-free | 0.27850 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1l9v |
RMSD bond length | 0.007 |
RMSD bond angle | 1.198 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.700 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.062 | 0.400 |
Number of reflections | 13859 | |
<I/σ(I)> | 15.2 | 2.9 |
Redundancy | 8.01 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 298 | Protein:precipitant ratio 1:1 ;precipitant: 15% PEG 6000, 0.2M Magnesium acetate, 0.1M Tris-HCl; Protein buffer 0.2M MgCl2, 0.5mM EDTA, 0.5mM DTT, 2mM Tris-HCl, pH7.3, VAPOR DIFFUSION, HANGING DROP, temperature 298K |