1GZO
Structure of protein kinase B unphosphorylated
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 | 149.703, 149.703, 39.185 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.000 * - 2.750 |
R-factor | 0.248 |
Rwork | 0.248 |
R-free | 0.30000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cdk |
RMSD bond length | 0.011 |
RMSD bond angle | 1.570 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.850 |
High resolution limit [Å] | 2.700 * | 2.750 |
Rmerge | 0.065 * | 0.236 * |
Total number of observations | 50875 * | |
Number of reflections | 12147 | |
<I/σ(I)> | 18 | |
Completeness [%] | 94.2 | 84 |
Redundancy | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8.5 * | 20 * | 30% PEG 8000, 0.2 M LITHIUM SULPHATE, 0.1 M TRIS, 10MG/ML PROTEIN, 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) |