3MUP
cIAP1-BIR3 domain in complex with the Smac-mimetic compound Smac037
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 70 |
| Detector technology | CCD |
| Collection date | 2009-11-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.94 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 71.630, 79.790, 98.410 |
| Unit cell angles | 90.00, 92.48, 90.00 |
Refinement procedure
| Resolution | 53.270 - 2.600 |
| R-factor | 0.229 |
| Rwork | 0.226 |
| R-free | 0.28760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3d9u chain A |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.060 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.270 | 2.740 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.093 | 0.369 |
| Number of reflections | 15911 | |
| <I/σ(I)> | 5.5 | 2 |
| Completeness [%] | 93.3 | 96.3 |
| Redundancy | 2.3 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293.15 | 25% PEG 3350, 0.1M HEPES pH 7.5, 0.2M Litium Sulphate; Drop volume: 0.3ul; Protein proportion: 67%; Protein concentration: 10 mg/ml, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |
