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1H27

CDK2/CyclinA in complex with an 11-residue recruitment peptide from p27

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Detector technologyCCD
DetectorADSC CCD
Wavelength(s)0.933
Spacegroup nameP 21 21 21
Unit cell lengths73.687, 133.547, 148.081
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution29.600

*

- 2.200
R-factor0.229
Rwork0.227
R-free0.26100

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qmz
RMSD bond length0.008

*

RMSD bond angle1.190

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.9902.320
High resolution limit [Å]2.2002.200
Rmerge0.0730.399
Total number of observations181975

*

Number of reflections63569
<I/σ(I)>6.41.4
Completeness [%]98.798.7
Redundancy2.62.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

7.4

*

0.8M KCL, 1.2M (NH4)2SO4, 40MM HEPES PH 7.0. PROTIEN 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 2024-10-30

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