5E0H
1.95 A resolution structure of Norovirus 3CL protease in complex with a triazole-based macrocyclic (18-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 | 2013-04-13 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 |
Unit cell lengths | 38.102, 48.772, 53.083 |
Unit cell angles | 94.00, 109.50, 101.29 |
Refinement procedure
Resolution | 37.010 - 1.950 |
R-factor | 0.1846 |
Rwork | 0.183 |
R-free | 0.21870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ur9 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.136 |
Data reduction software | XDS |
Data scaling software | Aimless (0.1.29) |
Phasing software | PHASER (2.5.2) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 37.010 | 37.010 | 2.000 |
High resolution limit [Å] | 1.950 | 8.940 | 1.950 |
Rmerge | 0.046 | 0.022 | 0.442 |
Rpim | 0.046 | 0.022 | 0.442 |
Total number of observations | 43724 | 485 | 3031 |
Number of reflections | 24256 | ||
<I/σ(I)> | 8 | 22 | 1.7 |
Completeness [%] | 95.2 | 95.4 | 94 |
Redundancy | 1.8 | 1.9 | 1.8 |
CC(1/2) | 0.997 | 0.998 | 0.755 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 20% w/v PEG3350, 200 mM sodium thiocyanate |