4XBB
1.85A resolution structure of Norovirus 3CL protease complex with a covalently bound dipeptidyl inhibitor diethyl [(1R,2S)-2-[(N-{[(3-chlorobenzyl)oxy]carbonyl}-3-cyclohexyl-L-alanyl)amino]-1-hydroxy-3-(2-oxo-2H-pyrrol-3-yl)propyl]phosphonate
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 | 2014-04-17 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0000 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 124.171, 124.171, 49.969 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.316 - 1.850 |
R-factor | 0.1641 |
Rwork | 0.163 |
R-free | 0.19650 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ur9 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.229 |
Data scaling software | Aimless (0.2.17) |
Phasing software | PHASER (2.5.6) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 45.320 | 45.320 | 1.890 |
High resolution limit [Å] | 1.850 | 9.060 | 1.850 |
Rmerge | 0.197 | 0.051 | 1.505 |
Total number of observations | 384657 | 3510 | 22129 |
Number of reflections | 19899 | ||
<I/σ(I)> | 14.9 | 46.1 | 2.4 |
Completeness [%] | 100.0 | 99.5 | 100 |
Redundancy | 19.3 | 16 | 18.5 |
CC(1/2) | 0.998 | 0.999 | 0.763 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 293 | 20% (w/v) PEG 5000 MME, 100 mM Tris, 200 mM ammonium sulfate |