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1E9N

A second divalent metal ion in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1, and its implications for the catalytic mechanism

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL11-1
Synchrotron siteSSRL
BeamlineBL11-1
Temperature [K]110
Detector technologyCCD
Collection date1999-07-15
DetectorADSC CCD
Spacegroup nameC 1 2 1
Unit cell lengths137.522, 45.016, 125.702
Unit cell angles90.00, 108.03, 90.00
Refinement procedure
Resolution20.000 - 2.200
Rwork0.186
R-free0.25200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)TO BE PUBLISHED
RMSD bond length0.018
RMSD bond angle18.920

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareEPMR
Refinement softwareTNT (5F)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]67.4202.320
High resolution limit [Å]2.2002.200
Rmerge0.082

*

0.379
Total number of observations102875

*

Number of reflections34905
<I/σ(I)>11.82.1
Completeness [%]93.070.5
Redundancy2.92
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.54

*

HANGING DROP, DROP 2+2 UL, 15MG/ML PROTEIN, 1 ML WELL, 0.1M TRIS-HCL, PH 7.5, 0.2M NAOAC, 30% PEG4K, 20MM HECAMEG, 1MM PB(OAC)2, 1MM DTT
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10-12 (mg/ml)
21reservoirTris-HCl0.1 (M)
31reservoirsodium acetate0.2 (M)
41reservoirPEG400025 (%)
51reservoirlead (II) acetate1 (mM)
61reservoirHECAMEG19.5 (mM)

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