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1OL7

Structure of Human Aurora-A 122-403 phosphorylated on Thr287, Thr288

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-1
Synchrotron siteESRF
BeamlineID14-1
Temperature [K]100
Detector technologyCCD
Collection date2003-05-15
DetectorADSC CCD
Spacegroup nameP 61 2 2
Unit cell lengths81.180, 81.180, 169.620
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution20.000 - 2.750
R-factor0.257
Rwork0.257
R-free0.29600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)UNPHOSPHORYLATED AURORA-A
RMSD bond length0.020
RMSD bond angle2.240
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareCNS
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]70.0002.900
High resolution limit [Å]2.7502.750
Rmerge0.1190.346
Number of reflections9235
<I/σ(I)>3.82.1
Completeness [%]100.0100
Redundancy10.110.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

8.5USING 20% PEG300, 5% PEG8000, 100 MM TRIS 8.5, 10% GLYCEROL, pH 8.50
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG30020 (%)
21reservoirPEG80005 (%)
31reservoirTris100 (mM)pH8.5
41reservoirglycerol10 (%)
51dropprotein9 (mg/ml)
61dropATPgammaS2 (mM)
71drop2 (mM)

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PDB entries from 2024-05-15

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