1QN4
Crystal structure of the T(-24) 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 method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 100 |
| Detector technology | AREA DETECTOR |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.000, 57.000, 147.000 |
| Unit cell angles | 90.00, 96.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.860 |
| R-factor | 0.21 |
| Rwork | 0.210 |
| R-free | 0.26400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PLANT TBP-ADMLP TATA DNA |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 15.000 |
| High resolution limit [Å] | 1.860 |
| Rmerge | 0.042 * |
| Number of reflections | 57768 |
| Completeness [%] | 96.5 |
| Redundancy | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 5.9 * | 4 * | pH 6.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | complex | 0.5 (mM) | |
| 2 | 1 | drop | MES | 40 (mM) | |
| 3 | 1 | drop | 60 (mM) | or 100 mM | |
| 4 | 1 | drop | 4 (mM) | ||
| 5 | 1 | drop | glycerol | 14 (%(v/v)) | |
| 6 | 1 | drop | ammonium acetate | 300 (mM) | |
| 7 | 1 | drop | dithiothreitol | 10 (mM) | |
| 8 | 1 | reservoir | MES | 12 (%(v/v)) | |
| 9 | 1 | reservoir | dithiothreitol | 10 (mM) |
