3O96
Crystal Structure of Human AKT1 with an Allosteric Inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-05-22 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.310, 69.940, 61.850 |
Unit cell angles | 90.00, 100.60, 90.00 |
Refinement procedure
Resolution | 24.700 - 2.700 |
R-factor | 0.249 |
Rwork | 0.245 |
R-free | 0.30800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | CODES 1MRV and 1UNP |
RMSD bond length | 0.005 |
RMSD bond angle | 0.900 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | CNX (2005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.850 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.078 | 0.382 |
Number of reflections | 11462 | |
<I/σ(I)> | 8.1 | 2 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 3.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 293 | 50 mM acetate-citrate buffer, 21% PEG MME 2000, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |