2BIY
Structure of PDK1-S241A mutant kinase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-02-04 |
| Detector | ADSC CCD |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 121.827, 121.827, 47.750 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 25.000 - 1.950 |
| R-factor | 0.186 |
| Rwork | 0.185 |
| R-free | 0.23000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h1w |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.512 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.080 | 0.420 |
| Number of reflections | 28782 | |
| <I/σ(I)> | 14.2 | 2.3 |
| Completeness [%] | 90.5 | 99.2 |
| Redundancy | 4.3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 2.2 M AMMONIUM SULPHATE, 0.1 M TRIS PH7.5, pH 7.50 |
