5WQT
Structure of a protein involved in pyroptosis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-06-08 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.886, 86.165, 112.145 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 68.330 - 2.640 |
| R-factor | 0.238 |
| Rwork | 0.235 |
| R-free | 0.28560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5b5r |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.417 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 68.330 | 2.700 |
| High resolution limit [Å] | 2.640 | 2.640 |
| Rmerge | 0.194 | 0.694 |
| Number of reflections | 13984 | |
| <I/σ(I)> | 13.25 | 2.22 |
| Completeness [%] | 98.0 | 97.6 |
| Redundancy | 6.4 | 6 |
| CC(1/2) | 0.911 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7 | 291 | 20mM Sodium bromide, 0.1M Hepes sodium pH7.0, 1.5M Sodium citrate tribasic dihydrate |
