1MRV
crystal structure of an inactive Akt2 kinase domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 170 |
Detector technology | CCD |
Collection date | 2001-03-15 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 150.440, 150.440, 40.180 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 2.800 |
Rwork | 0.247 |
R-free | 0.30700 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PKA in ternary complex |
RMSD bond length | 0.009 |
RMSD bond angle | 1.430 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 100.000 |
High resolution limit [Å] | 2.800 * |
Rmerge | 0.071 * |
Total number of observations | 50158 * |
Number of reflections | 11257 * |
<I/σ(I)> | 8.7 |
Completeness [%] | 94.4 * |
Redundancy | 3.97 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 4 * | Li2SO4, PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris | 100 (mM) | pH8.5 |
3 | 1 | drop | 150 (mM) | ||
4 | 1 | drop | glycerol | 10 (%) | |
5 | 1 | drop | beta-mercaptoethanol | 14 (mM) | |
6 | 1 | reservoir | Tris | 100 (mM) | pH8.5 |
7 | 1 | reservoir | 200 (mM) | ||
8 | 1 | reservoir | PEG4000 | 15 (%) |