4CEG
Crystal structure of Aurora A 122-403 C290A, C393A bound to ADP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04-1 |
Synchrotron site | Diamond |
Beamline | I04-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-10-27 |
Detector | DECTRIS PILATUS 2M |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 80.950, 80.950, 174.530 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 70.105 - 2.100 |
R-factor | 0.2017 |
Rwork | 0.200 |
R-free | 0.23750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ol7 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.223 |
Data reduction software | xia2 |
Data scaling software | xia2 |
Phasing software | PHENIX |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.100 | 2.150 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.050 | 0.670 |
Number of reflections | 20591 | |
<I/σ(I)> | 36.8 | 4.6 |
Completeness [%] | 99.9 | 99.6 |
Redundancy | 19.2 | 17.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | PROTEIN WAS CRYSTALLISED IN 0.1 M TRIS-HCL PH 8.5, 0.2 M MGCL2, 0.5 M NACL, 32.5 % PEG 3350 AFTER INCUBATION WITH 5 MM ADP/MGCL2 BY VAPOUR DIFFUSION |