3S5B
Crystal Structure of CED-3 Protease Suppressor-6 (CPS-6) from Caenorhabditis elegans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2010-01-31 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.221, 45.379, 80.310 |
| Unit cell angles | 90.00, 104.17, 90.00 |
Refinement procedure
| Resolution | 37.593 - 1.796 |
| R-factor | 0.168 |
| Rwork | 0.166 |
| R-free | 0.20990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.043 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.6_289) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.796 | 4.880 | 1.800 |
| Rmerge | 0.027 | 0.348 | |
| Number of reflections | 44074 | ||
| <I/σ(I)> | 11.6 | ||
| Completeness [%] | 97.2 | 97.5 | 100 |
| Redundancy | 3 | 2.9 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 277 | 6% Tacsimate, 0.1M MES, 25% PEG4000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
