8E6C
Crystal structure of MERS 3CL protease in complex with a m-fluorophenyl dimethyl sulfane inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 19-ID |
Synchrotron site | NSLS-II |
Beamline | 19-ID |
Temperature [K] | 291 |
Detector technology | PIXEL |
Collection date | 2022-06-06 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.9786 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 100.960, 57.400, 49.750 |
Unit cell angles | 90.00, 112.42, 90.00 |
Refinement procedure
Resolution | 46.660 - 2.700 |
R-factor | 0.2036 |
Rwork | 0.201 |
R-free | 0.25870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5wkk |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.7) |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.890 | 48.890 | 2.770 |
High resolution limit [Å] | 2.700 | 12.080 | 2.700 |
Rmerge | 0.147 | 0.038 | 0.728 |
Rmeas | 0.174 | 0.047 | 0.855 |
Rpim | 0.093 | 0.026 | 0.446 |
Total number of observations | 25099 | 262 | 2026 |
Number of reflections | 7324 | 90 | 560 |
<I/σ(I)> | 5.3 | 11.6 | 1.4 |
Completeness [%] | 99.7 | 97.5 | 99.8 |
Redundancy | 3.4 | 2.9 | 3.6 |
CC(1/2) | 0.989 | 0.997 | 0.597 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 25% (w/v) PEG 3350, 100 mM Tris, 200 mM magnesium chloride |