4ZNX
Crystal structure of the Fyn-SH3 domain in complex with the high affinity peptide APP12
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-11-22 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97626 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 31.658, 76.664, 73.175 |
Unit cell angles | 90.00, 94.74, 90.00 |
Refinement procedure
Resolution | 19.858 - 2.100 |
R-factor | 0.1817 |
Rwork | 0.179 |
R-free | 0.22230 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ua6 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.181 |
Data reduction software | autoPROC |
Data scaling software | Aimless (0.5.1) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 19.860 | 19.860 | 2.160 |
High resolution limit [Å] | 2.100 | 8.910 | 2.100 |
Rmerge | 0.092 | 0.112 | 0.636 |
Rpim | 0.035 | 0.044 | 0.356 |
Total number of observations | 153807 | 1798 | 5176 |
Number of reflections | 20052 | ||
<I/σ(I)> | 16.6 | 51.2 | 3 |
Completeness [%] | 98.2 | 91.5 | 84.6 |
Redundancy | 7.7 | 6.8 | 3.7 |
CC(1/2) | 0.998 | 0.996 | 0.785 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 4 M sodium formate, 0.1 M Hepes |