5TG2
1.75 A resolution structure of Norovirus 3CL protease in complex with the a n-pentyl substituted macrocyclic inhibitor (17-mer)
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 | 2016-08-14 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.00000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 67.020, 36.703, 61.721 |
Unit cell angles | 90.00, 110.23, 90.00 |
Refinement procedure
Resolution | 32.790 - 1.750 |
R-factor | 0.1781 |
Rwork | 0.176 |
R-free | 0.22680 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5e0g |
RMSD bond length | 0.010 |
RMSD bond angle | 0.998 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.27) |
Phasing software | PHASER (2.6.1) |
Refinement software | PHENIX (dev_2502) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 32.790 | 32.790 | 1.780 |
High resolution limit [Å] | 1.750 | 9.090 | 1.750 |
Rmerge | 0.082 | 0.029 | 0.464 |
Total number of observations | 46353 | ||
Number of reflections | 14350 | ||
<I/σ(I)> | 9.5 | ||
Completeness [%] | 99.6 | 99 | 94.6 |
Redundancy | 3.2 | 3.1 | 2.4 |
CC(1/2) | 0.996 | 0.998 | 0.780 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 28% (w/v) Polyethylene glycol monomethyl ether 2,000, 100 mM Bis-Tris |