5K26
Structure of the SH3 domain of MLK3 bound to peptide generated from phage display
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-03-25 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.978720 |
Spacegroup name | P 31 |
Unit cell lengths | 64.000, 64.000, 35.200 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 55.430 - 1.200 |
R-factor | 0.13865 |
Rwork | 0.137 |
R-free | 0.16826 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1sem |
RMSD bond length | 0.035 |
RMSD bond angle | 3.006 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.430 | 1.270 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.042 | 0.418 |
Number of reflections | 48242 | |
<I/σ(I)> | 19.53 | 2.76 |
Completeness [%] | 97.2 | 83.1 |
Redundancy | 4.92 | 2.55 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 0.1 M Na-Phosphate, 0.1 M K-Phosphate, 0.1 M MES 6.5, 1.5 M NaCl |