5E0G
1.20 A resolution structure of Norovirus 3CL protease in complex with a triazole-based macrocyclic (17-mer) inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-04-09 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 65.842, 39.281, 61.318 |
Unit cell angles | 90.00, 108.73, 90.00 |
Refinement procedure
Resolution | 31.178 - 1.200 |
R-factor | 0.1394 |
Rwork | 0.138 |
R-free | 0.16140 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ur9 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.109 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.7) |
Phasing software | PHASER (2.5.7) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 33.240 | 33.240 | 1.220 |
High resolution limit [Å] | 1.200 | 6.570 | 1.200 |
Rmerge | 0.037 | 0.029 | 0.580 |
Total number of observations | 147835 | 962 | 6758 |
Number of reflections | 44826 | ||
<I/σ(I)> | 14.1 | 36 | 2.1 |
Completeness [%] | 96.7 | 96.4 | 94.2 |
Redundancy | 3.3 | 3.2 | 3.2 |
CC(1/2) | 0.999 | 0.997 | 0.758 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 30% w/v PEG2000 MME, 150 mM potassium bromide |