3D9T
CIAP1-BIR3 in complex with N-terminal peptide from Caspase-9 (ATPFQE)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-01-01 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 30.268, 68.427, 122.358 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.040 - 1.500 |
| R-factor | 0.186 |
| Rwork | 0.183 |
| R-free | 0.20500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nw9 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | CNX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 61.200 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.052 | 0.257 |
| Number of reflections | 40966 | |
| <I/σ(I)> | 35.4 | 5.5 |
| Completeness [%] | 98.0 | 98.6 |
| Redundancy | 6.4 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 3.1M NA FORMATE,10% GLYCEROL,1.5MM PEPTIDE, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
