7ARA
Rhinovirus A2 2A protease in complex with zVAM.fmk
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-02-01 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 74.647, 74.647, 160.831 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 60.000 - 2.243 |
| R-factor | 0.2162 |
| Rwork | 0.214 |
| R-free | 0.25720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2hrv |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.973 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (v1.17.1-3660) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 64.646 | 64.646 | 2.546 |
| High resolution limit [Å] | 2.243 | 8.188 | 2.243 |
| Rmerge | 0.188 | 0.050 | 2.074 |
| Rmeas | 0.194 | 0.052 | 2.131 |
| Rpim | 0.044 | 0.013 | 0.484 |
| Total number of observations | 232197 | 10517 | 11545 |
| Number of reflections | 12111 | 604 | 608 |
| <I/σ(I)> | 12.9 | 38.3 | 1.8 |
| Completeness [%] | 93.3 | 99.8 | 80.3 |
| Redundancy | 19.2 | 17.4 | 19 |
| CC(1/2) | 0.998 | 0.998 | 0.583 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277.15 | 7.5 % PEG8000, 0.3 M KCNS, 5 % 2-methyl-2-butanol, 10 % glycerol, 10 mM b-mercaptoethanol and 50 mM sodium-potassium phosphate buffer pH 8.0 |
