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1H25

CDK2/Cyclin A in complex with an 11-residue recruitment peptide from retinoblastoma-associated protein

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 lengths73.609, 133.851, 147.910
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000

*

- 2.500
R-factor0.249
Rwork0.249
R-free0.29600

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qmz
RMSD bond length0.012

*

RMSD bond angle1.380

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.9902.590
High resolution limit [Å]2.5002.500
Rmerge0.0920.439
Total number of observations252831

*

Number of reflections52141
<I/σ(I)>6.21.7
Completeness [%]100.0100
Redundancy4.84.6
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

218853

数据于2024-04-24公开中

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