4WCI
Crystal structure of the 1st SH3 domain from human CD2AP (CMS) in complex with a proline-rich peptide (aa 378-393) from human RIN3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-12-20 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.9173 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 95.526, 55.362, 64.557 |
| Unit cell angles | 90.00, 131.72, 90.00 |
Refinement procedure
| Resolution | 48.186 - 1.650 |
| R-factor | 0.1938 |
| Rwork | 0.192 |
| R-free | 0.21880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2j6f |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.010 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.190 | 1.740 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.132 | 0.479 |
| Number of reflections | 29622 | |
| <I/σ(I)> | 6.6 | 2.4 |
| Completeness [%] | 97.7 | 93 |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M Ca(ac) pH 4.2, 0.2 M Li2SO4 and 25% PEG 10 000 |
