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 |
