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1BIX

THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH2R
Temperature [K]110
Detector technologyIMAGE PLATE
Collection date1996-12
DetectorRIGAKU
Spacegroup nameC 1 2 1
Unit cell lengths87.260, 44.701, 78.778
Unit cell angles90.00, 103.45, 90.00
Refinement procedure
Resolution20.000 - 2.200
R-factor0.184
Rwork0.184
R-free0.26900
Structure solution methodMULTIPLE ISOMORPHOUS REPLACEMENT AND ANOMALOUS SCATTERING
RMSD bond length0.016
RMSD bond angle25.340

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareX-PLOR (3.84)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.310
High resolution limit [Å]2.2002.190
Rmerge0.0430.114
Total number of observations54729

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Number of reflections15089
<I/σ(I)>12.72.2
Completeness [%]98.190
Redundancy3.63
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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7.4drop consists of equal volume of protein and reservoir solutions

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropHEPES10 (mM)
31reservoirPEG800016-20 (%(w/v))
41reservoirMES100 (mM)
51reservoir1,4-Dioxane5 (%(v/v))
61reservoirsamarium acetate7.5-30 (mM)

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