3EG1
Crystal structure of the N114Q mutant of ABL-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-12-19 |
| Detector | BRUKER SMART 6000 |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.996, 47.636, 55.662 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.000 - 1.850 |
| R-factor | 0.192 |
| Rwork | 0.185 |
| R-free | 0.24800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o88 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 2.106 |
| Data reduction software | SAINT |
| Data scaling software | SAINT |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.636 | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.065 | 0.243 |
| Number of reflections | 10158 | |
| <I/σ(I)> | 3.49 | |
| Completeness [%] | 92.8 | 72.5 |
| Redundancy | 7.6 | 1.26 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 3.5 | 288 | 2M ammonium sulphate, 0.4 M NaCl, 0.1 M sodium citrate, 10% glycerol, pH 3.5, vapor diffusion, hanging drop, temperature 288K |
