4XBC
1.60 A resolution structure of Norovirus 3CL protease complex with a covalently bound dipeptidyl inhibitor (1R,2S)-2-({N-[(benzyloxy)carbonyl]-3-cyclohexyl-L-alanyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid (Hexagonal Form)
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 | 2012-11-12 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0000 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 121.853, 121.853, 51.498 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 36.854 - 1.600 |
R-factor | 0.1639 |
Rwork | 0.163 |
R-free | 0.17470 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.234 |
Data scaling software | Aimless (0.1.27) |
Phasing software | PHASER (2.5.3) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.280 | 46.280 | 1.630 |
High resolution limit [Å] | 1.600 | 8.760 | 1.600 |
Rmerge | 0.166 | 0.043 | 1.692 |
Total number of observations | 579016 | 3544 | 24787 |
Number of reflections | 30219 | ||
<I/σ(I)> | 16.3 | 53.3 | 2 |
Completeness [%] | 100.0 | 99.2 | 100 |
Redundancy | 19.2 | 15 | 16.9 |
CC(1/2) | 0.999 | 0.999 | 0.711 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 293 | 20% (w/v) PEG3350, 200 mM ammonium citrate |