1OL5
Structure of Aurora-A 122-403, phosphorylated on Thr287, Thr288 and bound to TPX2 1-43
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Collection date | 2003-04-15 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.630, 81.720, 83.050 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.500 |
| R-factor | 0.194 |
| Rwork | 0.194 |
| R-free | 0.25200 |
| Structure solution method | MAD |
| Starting model (for MR) | UNPHOSPHORYLATED AURORA/TPX2 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.700 |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.099 | 0.248 |
| Number of reflections | 14609 | |
| <I/σ(I)> | 5.1 | 1.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.6 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 | 18 * | 18% (W/V) PEG8000, 100 MM MES PH 6.5, 200 MM MGSO4 |
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) |
