5OB1
Crystal structure of the c-Src-SH3 domain Q128R mutant 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 | 2013-02-24 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9334 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 65.800, 32.840, 31.580 |
Unit cell angles | 90.00, 104.39, 90.00 |
Refinement procedure
Resolution | 22.433 - 1.172 |
R-factor | 0.1202 |
Rwork | 0.119 |
R-free | 0.14130 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4jz4 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.187 |
Data reduction software | XDS |
Data scaling software | Aimless (0.3.6) |
Phasing software | PHASER |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 22.433 | 22.433 | 1.190 |
High resolution limit [Å] | 1.170 | 6.420 | 1.170 |
Rmerge | 0.048 | 0.042 | 0.096 |
Rmeas | 0.058 | 0.052 | 0.119 |
Rpim | 0.033 | 0.032 | 0.069 |
Number of reflections | 42089 | ||
<I/σ(I)> | 17.7 | ||
Completeness [%] | 97.9 | 64.1 | 87.1 |
Redundancy | 2.9 | 2.3 | 2.5 |
CC(1/2) | 0.995 | 0.991 | 0.981 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 298 | 1.6 M Ammonium sulphate, 0.1 M sodium chloride, 0.1 M sodium acetate and 10% Glycerol |