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1H24

CDK2/CyclinA in complex with a 9 residue recruitment peptide from E2F

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-1
Synchrotron siteESRF
BeamlineID14-1
Temperature [K]100
Detector technologyCCD
Collection date2001-11-15
DetectorADSC CCD
Spacegroup nameP 21 21 21
Unit cell lengths73.551, 133.549, 147.890
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution100.000

*

- 2.500
R-factor0.212
Rwork0.209
R-free0.27000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qmz
RMSD bond length0.018

*

RMSD bond angle1.850

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.8002.560
High resolution limit [Å]2.5002.500
Rmerge0.0620.443
Total number of observations124102

*

Number of reflections48503
<I/σ(I)>8.81.7
Completeness [%]95.694.4
Redundancy2.62.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

7.4

*

0.8M KCL, 1.2M (NH4)2SO4, 40MM HEPES PH 7.0. PROTEIN CONCENTRATION = 10MG/ML
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropHEPES10 (mM)pH7.4
31drop150 (mM)
41dropEDTA3.4 (mM)
51dropazide0.01 (%)
61dropmonothiglycerol0.01 (%)
71reservoir0.8 (M)
81reservoirammonium sulfate1.2 (M)
91reservoirHEPES100 (mM)pH7.0

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PDB entries from 2024-03-27

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