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1QN5

Crystal structure of the G(-26) 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 detailsNSLS BEAMLINE X25
Synchrotron siteNSLS
BeamlineX25
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 - 1.930
R-factor0.196
Rwork0.196
R-free0.25200
Structure solution methodOTHER
RMSD bond length0.008
RMSD bond angle1.400
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]1.930
Rmerge0.050

*

Number of reflections51549
Completeness [%]98.7
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 2025-12-03

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