5TG1
1.40 A resolution structure of Norovirus 3CL protease in complex with the a m-chlorophenyl 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 | 2015-06-13 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.00000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 64.397, 36.495, 61.474 |
Unit cell angles | 90.00, 112.50, 90.00 |
Refinement procedure
Resolution | 31.829 - 1.400 |
R-factor | 0.1448 |
Rwork | 0.142 |
R-free | 0.19190 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ur9 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.035 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.9) |
Phasing software | PHASER (2.5.7) |
Refinement software | PHENIX (dev_2075) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 31.830 | 31.830 | 1.420 |
High resolution limit [Å] | 1.400 | 7.540 | 1.400 |
Rmerge | 0.048 | 0.031 | 0.691 |
Total number of observations | 83610 | ||
Number of reflections | 25218 | ||
<I/σ(I)> | 13.4 | ||
Completeness [%] | 96.8 | 97.8 | 95.3 |
Redundancy | 3.3 | 3.1 | 3.2 |
CC(1/2) | 0.998 | 0.998 | 0.704 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 30% (w/v) PEG 2000 MME, 150 potassium bromide |