6VH3
2.20 A resolution structure of MERS 3CL protease in complex with inhibitor 7j
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 | 2019-06-15 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.629, 90.960, 100.030 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.827 - 2.200 |
| R-factor | 0.1859 |
| Rwork | 0.183 |
| R-free | 0.24530 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5wkk |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (1.16_3544) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.480 | 2.270 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.141 | 1.040 |
| Total number of observations | 238120 | 20362 |
| Number of reflections | 35788 | 3067 |
| <I/σ(I)> | 9.3 | 1.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.7 | 6.6 |
| CC(1/2) | 0.996 | 0.740 |
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 |
