9ESA
Aurora-C with SER mutation in complex with INCENP peptide
This is a non-PDB format compatible entry.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-04-20 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5405 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 79.280, 79.490, 265.240 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.870 - 2.800 |
R-factor | 0.2313 |
Rwork | 0.228 |
R-free | 0.29400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 1.279 |
Data reduction software | CrystalClear (1.3.6sp3) |
Data scaling software | CrystalClear (1.3.6sp3) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.870 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.126 | 0.350 |
Number of reflections | 21012 | 2057 |
<I/σ(I)> | 6.1 | 2.3 |
Completeness [%] | 99.6 | 99.9 |
Redundancy | 4.8 | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 0.1 M Bis-Tris pH5.5, 0.025-0.05 M ammonium sulphate, 9-12% PEG3350 |