7DA6
Enterovirus 71 2A Protease mutant- C110A in complex with peptide inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE TPS 05A |
| Synchrotron site | NSRRC |
| Beamline | TPS 05A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2019-12-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.99984 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 85.476, 44.407, 51.369 |
| Unit cell angles | 90.00, 111.57, 90.00 |
Refinement procedure
| Resolution | 22.754 - 2.200 |
| R-factor | 0.1923 |
| Rwork | 0.186 |
| R-free | 0.24370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fvb |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.224 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4-1496) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 5.960 | 2.200 |
| Rmerge | 0.063 | 0.043 | 0.312 |
| Rmeas | 0.075 | 0.050 | 0.367 |
| Rpim | 0.039 | 0.027 | 0.192 |
| Total number of observations | 32175 | ||
| Number of reflections | 9107 | 477 | 445 |
| <I/σ(I)> | 9.8 | ||
| Completeness [%] | 98.9 | 96.6 | 98.7 |
| Redundancy | 3.5 | 3.4 | 3.5 |
| CC(1/2) | 0.995 | 0.882 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 296 | 0.1 M HEPES (pH 7.5), 20% 2-propanol, and 10% polyethylene glycol (PEG) 4000 |
