6WLY
PAK4 kinase domain in complex with LIMK1 Thr508 substrate peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-07-07 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9792 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 61.626, 61.626, 179.596 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.580 - 1.900 |
R-factor | 0.1871 |
Rwork | 0.186 |
R-free | 0.20530 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4fij |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER (2.8.1) |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 4.090 | 1.900 |
Rmerge | 0.140 | 0.122 | 1.502 |
Rmeas | 0.143 | 0.125 | 1.553 |
Rpim | 0.030 | 0.027 | 0.386 |
Total number of observations | 576393 | ||
Number of reflections | 28404 | 3106 | 2747 |
<I/σ(I)> | 6.8 | ||
Completeness [%] | 99.9 | 99.6 | 99.9 |
Redundancy | 20.3 | 20.9 | 15.3 |
CC(1/2) | 0.996 | 0.615 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 0.1M Tris-HCl, 2M Na acetate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K, 2mM peptide |