9ATH
Crystal structure of MERS 3CL protease in complex with a methylbicyclo[2.2.1]heptene 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 | 49.807, 106.232, 58.215 |
| Unit cell angles | 90.00, 109.23, 90.00 |
Refinement procedure
| Resolution | 47.030 - 1.650 |
| R-factor | 0.1834 |
| Rwork | 0.182 |
| R-free | 0.20850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.884 |
| 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] | 106.230 | 1.690 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.108 | 1.093 |
| Rmeas | 0.124 | 1.243 |
| Rpim | 0.060 | 0.585 |
| Total number of observations | 289398 | 21944 |
| Number of reflections | 68325 | 5035 |
| <I/σ(I)> | 8.8 | 1.5 |
| Completeness [%] | 99.6 | |
| Redundancy | 4.2 | 4.4 |
| CC(1/2) | 0.997 | 0.476 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 800 mM potassium sodium tartrate tetrahydrate, 100 mM Tris, pH 8.5, 0.5% w/v PEG5000 MME |
