8CZT
Structure of MERS 3CL protease in complex with the cyclopropane based inhibitor 15d
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 | 101.619, 56.935, 49.830 |
Unit cell angles | 90.00, 112.41, 90.00 |
Refinement procedure
Resolution | 48.690 - 2.100 |
R-factor | 0.2032 |
Rwork | 0.200 |
R-free | 0.26170 |
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] | 48.690 | 48.690 | 2.150 |
High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
Rmerge | 0.066 | 0.023 | 0.359 |
Rmeas | 0.079 | 0.028 | 0.427 |
Rpim | 0.043 | 0.015 | 0.228 |
Total number of observations | 50621 | 585 | 3893 |
Number of reflections | 14941 | 183 | 1143 |
<I/σ(I)> | 10.6 | 30.4 | 2.9 |
Completeness [%] | 96.5 | 97 | 99.5 |
Redundancy | 3.4 | 3.2 | 3.4 |
CC(1/2) | 0.998 | 0.999 | 0.933 |
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 |