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1QN3

Crystal structure of the C(-25) Adenovirus major late promoter TATA box variant bound to wild-type TBP (Arabidopsis thaliana TBP isoform 2). TATA element recognition by the TATA box-binding protein has been conserved throughout evolution.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsCHESS BEAMLINE F1
Synchrotron siteCHESS
BeamlineF1
Temperature [K]100
Detector technologyAREA DETECTOR
Spacegroup nameP 1 21 1
Unit cell lengths41.800, 146.700, 57.400
Unit cell angles90.00, 90.50, 90.00
Refinement procedure
Resolution6.000 - 1.950
R-factor0.199
Rwork0.199
R-free0.25500
Structure solution methodOTHER
RMSD bond length0.009
RMSD bond angle1.500
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 Overall
Low resolution limit [Å]15.000
High resolution limit [Å]1.950
Number of reflections50342
Completeness [%]99.5
Redundancy4.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

5.9

*

4

*

pH 6.00
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropcomplex0.5 (mM)
101reservoirdithiothreitol10 (mM)
21dropMES40 (mM)
31drop60 (mM)or 100 mM
41drop4 (mM)
51dropglycerol14 (%(v/v))
61dropammonium acetate300 (mM)
71dropdithiothreitol10 (mM)
81reservoirglycerol12 (%(v/v))
91reservoirMES25 (mM)

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PDB entries from 2024-12-25

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