1UNQ
High resolution crystal structure of the Pleckstrin Homology Domain Of Protein Kinase B/Akt Bound To Ins(1,3,4,5)-Tetrakisphophate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-01-15 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 82.904, 34.388, 44.292 |
| Unit cell angles | 90.00, 115.29, 90.00 |
Refinement procedure
| Resolution | 15.000 - 0.980 |
| R-factor | 0.154 |
| R-free | 0.17900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h10 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 0.030 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.020 |
| High resolution limit [Å] | 0.980 | 0.980 |
| Rmerge | 0.064 | 0.557 |
| Number of reflections | 60005 | |
| <I/σ(I)> | 19.3 | 2.8 |
| Completeness [%] | 93.2 | 92.9 |
| Redundancy | 3.4 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 0.25 M AMMONIUM ACETATE, 30 % PEG 4000, 0.1 M SODIUM ACETATE (4.6), pH 4.60 |
