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 |
