5OB2
Crystal structure of the c-Src-SH3 domain E97T mutant in complex with the high affinity peptide APP12
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-1 |
Synchrotron site | ESRF |
Beamline | MASSIF-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-02-25 |
Detector | DECTRIS PILATUS 2M |
Wavelength(s) | 0.965 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 30.720, 31.704, 66.722 |
Unit cell angles | 90.00, 99.04, 90.00 |
Refinement procedure
Resolution | 19.288 - 1.800 |
R-factor | 0.1995 |
Rwork | 0.198 |
R-free | 0.21990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4jz4 |
RMSD bond length | 0.008 |
RMSD bond angle | 0.845 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.4) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 19.290 | 19.290 | 1.840 |
High resolution limit [Å] | 1.800 | 9.000 | 1.800 |
Rmerge | 0.059 | 0.039 | 0.244 |
Rmeas | 0.076 | 0.053 | 0.308 |
Rpim | 0.047 | 0.035 | 0.186 |
Number of reflections | 21432 | ||
<I/σ(I)> | 9.8 | ||
Completeness [%] | 93.1 | 82.1 | 96.6 |
Redundancy | 2.3 | 2.2 | 2.3 |
CC(1/2) | 0.994 | 0.991 | 0.931 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 298 | 1.9 M Ammonium sulphate, 0.1 M sodium acetate and 10% PEG 400 |