5X45
Crystal structure of 2A protease from Human rhinovirus C15
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-17A |
| Synchrotron site | Photon Factory |
| Beamline | BL-17A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-04-03 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 80.992, 85.370, 208.908 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.685 - 2.602 |
| R-factor | 0.1674 |
| Rwork | 0.165 |
| R-free | 0.21520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.112 |
| Data reduction software | SCALEPACK |
| Data scaling software | SCALEPACK |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 5.600 | 2.600 |
| Rmerge | 0.153 | 0.109 | 0.636 |
| Total number of observations | 200681 | ||
| Number of reflections | 22666 | ||
| <I/σ(I)> | 9.6 | ||
| Completeness [%] | 99.9 | 100 | 99.8 |
| Redundancy | 8.9 | 9.6 | 8.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289.15 | 0.2 M potassium chloride, 0.1 M magnesium acetate tetrahydrate, 0.05 M sodium cacodylate and 10% w/v PEG 8000 |
