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1H28

CDK2/CyclinA in complex with an 11-residue recruitment peptide from p107

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
Collection date2002-03-15
DetectorADSC CCD
Spacegroup nameP 21 21 2
Unit cell lengths149.503, 162.514, 71.375
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution29.600

*

- 2.800
R-factor0.247
Rwork0.243
R-free0.32700

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qmz
RMSD bond length0.014

*

RMSD bond angle1.840

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.9902.950
High resolution limit [Å]2.8002.800
Rmerge0.1660.617
Total number of observations92651

*

Number of reflections41507
<I/σ(I)>2.81.2
Completeness [%]95.797.8
Redundancy2.22.1
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

217705

数据于2024-03-27公开中

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