4J9C
Crystal structure of the Abl-SH3 domain H59Q-N96T mutant complexed with the designed high-affinity peptide ligand P17
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 | 2011-04-08 |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 32 1 2 |
| Unit cell lengths | 49.646, 49.646, 45.410 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 16.754 - 1.051 |
| R-factor | 0.1468 |
| Rwork | 0.146 |
| R-free | 0.16220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o88 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.237 |
| Data reduction software | XDS |
| Data scaling software | SCALA (0.1.30) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.995 | 1.110 |
| High resolution limit [Å] | 1.051 | 1.050 |
| Rmerge | 0.040 | 0.472 |
| Number of reflections | 29561 | |
| <I/σ(I)> | 28.7 | 4.61 |
| Completeness [%] | 98.8 | 99.1 |
| Redundancy | 8.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | 1.5 M AMS, 5% PEG 200, 20 mM LiCl, 0.1 M AcONa , pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
