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 |