1GZK
Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-09-15 |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 148.405, 148.405, 38.547 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.000 * - 2.300 |
R-factor | 0.248 |
Rwork | 0.248 |
R-free | 0.30900 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cdk |
RMSD bond length | 0.011 * |
RMSD bond angle | 1.540 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | |
High resolution limit [Å] | 2.300 | |
Rmerge | 0.050 | 0.243 * |
Total number of observations | 113677 * | |
Number of reflections | 18905 * | |
<I/σ(I)> | 21 | |
Completeness [%] | 96.1 | 77.8 * |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7.5 | 20 * | 10MG/ML PROTEIN, 30% PEG4K, 0.2 M LITHIUM SULPHATE, 0.1 M TRIS, pH 7.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 10 (mg/ml) | |
2 | 1 | 1 | AMP-PNP-MgCl2 | 5 (mM) | |
3 | 1 | 1 | PEG400 | 30 (%(w/v)) | |
4 | 1 | 1 | lithium sulfate | 0.2 (M) | |
5 | 1 | 1 | Tris-HCl | 0.1 (M) | pH8.5 |
6 | 1 | 1 | dithiothreitol | 5 (mM) |