6B6I
2.4A resolution structure of human Norovirus GII.4 protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-08-22 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 32 |
Unit cell lengths | 112.940, 112.940, 153.370 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 51.123 - 2.440 |
R-factor | 0.1816 |
Rwork | 0.180 |
R-free | 0.22200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2iph |
RMSD bond length | 0.008 |
RMSD bond angle | 1.207 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 52.990 | 2.500 |
High resolution limit [Å] | 2.440 | 2.440 |
Rmerge | 0.094 | 1.355 |
Number of reflections | 81454 | 6060 |
<I/σ(I)> | 10.4 | 1.2 |
Completeness [%] | 100.0 | 99.9 |
Redundancy | 6.4 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 287 | PEG 8000, Lithium Sulfate, Tris, MES, glycerol |