7T3Y
Structure of MERS 3CL protease in complex with inhibitor 8c
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 | 2021-07-29 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.232, 91.327, 99.170 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.660 - 1.900 |
| R-factor | 0.208 |
| Rwork | 0.205 |
| R-free | 0.25800 |
| 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 (1.20RC2_4402) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.660 | 45.660 | 1.940 |
| High resolution limit [Å] | 1.900 | 9.110 | 1.900 |
| Rmerge | 0.060 | 0.027 | 1.750 |
| Total number of observations | 369090 | 3436 | 24437 |
| Number of reflections | 54463 | 569 | 3471 |
| <I/σ(I)> | 14.8 | 50.6 | 1.4 |
| Completeness [%] | 99.9 | 98.8 | 99.6 |
| Redundancy | 6.8 | 6 | 7 |
| CC(1/2) | 0.999 | 0.999 | 0.723 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 20% (w/v) PEG 3350, 100 mM, 200 mM ammonium sulfate |
