8CZV
Structure of MERS 3CL protease in complex with the cyclopropane based inhibitor 17d
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] | 100 |
Detector technology | PIXEL |
Collection date | 2022-03-24 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.9795 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 101.470, 57.450, 49.858 |
Unit cell angles | 90.00, 112.47, 90.00 |
Refinement procedure
Resolution | 48.990 - 1.950 |
R-factor | 0.1871 |
Rwork | 0.184 |
R-free | 0.24170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5wkk |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.8) |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.990 | 48.990 | 2.000 |
High resolution limit [Å] | 1.950 | 8.940 | 1.950 |
Rmerge | 0.089 | 0.023 | 0.661 |
Total number of observations | 68418 | 756 | 4951 |
Number of reflections | 19345 | 220 | 1362 |
<I/σ(I)> | 9.8 | 35.7 | 1.8 |
Completeness [%] | 99.5 | 98.5 | 99.7 |
Redundancy | 3.5 | 3.4 | 3.6 |
CC(1/2) | 0.997 | 0.999 | 0.840 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 25% (w/v) PEG 3350, 100 mM Bis-Tris, 200 mM Ammonium Sulfate |