9ATE
Crystal structure of MERS 3CL protease in complex with a methylbicyclo[2.2.1]heptane 2-pyrrolidone inhibitor
This is a non-PDB format compatible entry.
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 | 2022-12-05 |
| Detector | DECTRIS EIGER2 XE 9M |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.847, 105.869, 57.751 |
| Unit cell angles | 90.00, 109.08, 90.00 |
Refinement procedure
| Resolution | 54.580 - 1.850 |
| R-factor | 0.1646 |
| Rwork | 0.163 |
| R-free | 0.19130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.976 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 105.870 | 1.900 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.072 | 1.062 |
| Rmeas | 0.078 | 1.152 |
| Rpim | 0.030 | 0.442 |
| Total number of observations | 331595 | 23552 |
| Number of reflections | 48244 | 3519 |
| <I/σ(I)> | 13.7 | 2 |
| Completeness [%] | 100.0 | |
| Redundancy | 6.9 | 6.7 |
| CC(1/2) | 0.999 | 0.679 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 25% w/v PEG3350, 100 mM HEPES, pH 7.5 |
