2Q0N
Structure of human p21 activating kinase 4 (PAK4) in complex with a consensus peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-03 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97910 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 145.678, 145.678, 39.577 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.580 - 1.750 |
| R-factor | 0.185 |
| Rwork | 0.182 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2j0i |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.588 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.057 | 0.355 |
| Number of reflections | 40410 | |
| <I/σ(I)> | 16.3 | |
| Completeness [%] | 92.5 | 94.2 |
| Redundancy | 12 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 1.7M Ammonium sulfate, 15% PEG400, 1M Tris-HCl pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
