4RTY
Crystal structure of the c-Src-SH3 domain in complex with the high affinity peptide APP12
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-11-04 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9334 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 65.910, 32.850, 31.640 |
| Unit cell angles | 90.00, 104.45, 90.00 |
Refinement procedure
| Resolution | 20.030 - 1.279 |
| R-factor | 0.117 |
| Rwork | 0.116 |
| R-free | 0.13710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4jz4 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.287 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.3.6) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.030 | 20.030 | 1.300 |
| High resolution limit [Å] | 1.280 | 6.770 | 1.280 |
| Rmerge | 0.049 | 0.052 | 0.181 |
| Total number of observations | 454 | 3387 | |
| Number of reflections | 17055 | ||
| <I/σ(I)> | 20.8 | 34.8 | 7.2 |
| Completeness [%] | 99.8 | 95.6 | 96.1 |
| Redundancy | 4.4 | 3.6 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 298 | 1.6M Ammonium sulphate, 0.1M sodium acetate and 10% Glycerol, pH 4.0, vapor diffusion, hanging drop, temperature 298K |
