8E6E
Crystal structure of MERS 3CL protease in complex with a phenyl 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 | 100.252, 58.087, 49.793 |
Unit cell angles | 90.00, 112.39, 90.00 |
Refinement procedure
Resolution | 46.040 - 1.500 |
R-factor | 0.174 |
Rwork | 0.173 |
R-free | 0.20300 |
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] | 49.220 | 49.220 | 1.540 |
High resolution limit [Å] | 1.500 | 6.710 | 1.500 |
Rmerge | 0.050 | 0.025 | 0.839 |
Rmeas | 0.059 | 0.030 | 1.027 |
Rpim | 0.031 | 0.016 | 0.582 |
Total number of observations | 148298 | 1738 | 8959 |
Number of reflections | 42253 | 494 | 3060 |
<I/σ(I)> | 11.6 | 41.8 | 1.3 |
Completeness [%] | 99.7 | 98.1 | 98.7 |
Redundancy | 3.5 | 3.5 | 2.9 |
CC(1/2) | 0.999 | 0.999 | 0.595 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | 25% (w/v) PEG 3350, 100 mM Bis-Tris |