1OL6
Structure of unphosphorylated D274N mutant of Aurora-A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Collection date | 2003-03-15 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 87.310, 87.310, 77.330 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 3.000 |
R-factor | 0.277 |
Rwork | 0.277 |
R-free | 0.30100 |
Structure solution method | MAD |
Starting model (for MR) | 1fot |
RMSD bond length | 0.015 |
RMSD bond angle | 1.936 |
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] | 58.000 | 3.160 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.165 | 0.432 |
Number of reflections | 12265 | |
<I/σ(I)> | 3.6 | 1.5 |
Completeness [%] | 98.4 | 98.4 |
Redundancy | 7.1 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 * | 18 * | 20% PEG3350, 190 MM NACL, 10 MM NAH2PO4, 100 MM TRIS PH 7.3 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 18 (%(w/v)) | |
2 | 1 | reservoir | MES | 100 (mM) | pH6.5 |
3 | 1 | reservoir | 200 (mM) | ||
4 | 1 | drop | protein | 20 (mg/ml) | |
5 | 1 | drop | ATPgammaS | 2 (mM) | |
6 | 1 | drop | 0.2 (mM) | ||
7 | 1 | drop | PEG8000 | 20 (%) | |
8 | 1 | drop | MES | 100 (mM) | pH6.5 |
9 | 1 | drop | 200 (mM) |