1OL7
Structure of Human Aurora-A 122-403 phosphorylated on Thr287, Thr288
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-05-15 |
Detector | ADSC CCD |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 81.180, 81.180, 169.620 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.750 |
R-factor | 0.257 |
Rwork | 0.257 |
R-free | 0.29600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | UNPHOSPHORYLATED AURORA-A |
RMSD bond length | 0.020 |
RMSD bond angle | 2.240 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.000 | 2.900 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.119 | 0.346 |
Number of reflections | 9235 | |
<I/σ(I)> | 3.8 | 2.1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 10.1 | 10.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8.5 | USING 20% PEG300, 5% PEG8000, 100 MM TRIS 8.5, 10% GLYCEROL, pH 8.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG300 | 20 (%) | |
2 | 1 | reservoir | PEG8000 | 5 (%) | |
3 | 1 | reservoir | Tris | 100 (mM) | pH8.5 |
4 | 1 | reservoir | glycerol | 10 (%) | |
5 | 1 | drop | protein | 9 (mg/ml) | |
6 | 1 | drop | ATPgammaS | 2 (mM) | |
7 | 1 | drop | 2 (mM) |