3Q53
Structure of phosphorylated PAK1 kinase domain in complex with ATP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-25 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9998 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 48.982, 103.588, 121.967 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.948 - 2.090 |
| R-factor | 0.1805 |
| Rwork | 0.178 |
| R-free | 0.22310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yhw |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.113 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.160 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Rmerge | 0.051 | 0.214 |
| Number of reflections | 18806 | |
| <I/σ(I)> | 12.38 | |
| Completeness [%] | 99.7 | 99.7 |
| Redundancy | 12.1 | 11.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 294 | 25% PEG 3350, 0.2M Na/K Tartrate, 0.1M NDSB256, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
