1I4E
CRYSTAL STRUCTURE OF THE CASPASE-8/P35 COMPLEX
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 32-ID |
| Synchrotron site | APS |
| Beamline | 32-ID |
| Wavelength(s) | 1.00 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 99.970, 117.340, 346.450 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.000 - 3.000 |
| Rwork | 0.236 |
| R-free | 0.29570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 24.483 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | GLRF |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 29.830 |
| High resolution limit [Å] | 3.000 |
| Rmerge | 0.089 |
| Number of reflections | 37662 |
| <I/σ(I)> | 18.3 |
| Completeness [%] | 91.9 |
| Redundancy | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 20 * | VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20-30 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | 150 (mM) | ||
| 4 | 1 | drop | dithiothreitol | 5 (mM) | |
| 5 | 1 | reservoir | PEG8000 | 2 (%) | |
| 6 | 1 | reservoir | MOPS | 100 (mM) | |
| 7 | 1 | reservoir | 2-propanol | 1 (%) |
