6PAX
CRYSTAL STRUCTURE OF THE HUMAN PAX-6 PAIRED DOMAIN-DNA COMPLEX REVEALS A GENERAL MODEL FOR PAX PROTEIN-DNA INTERACTIONS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS II |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 33.840, 61.686, 171.111 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.500 |
| R-factor | 0.233 |
| Rwork | 0.233 |
| R-free | 0.25600 |
| Structure solution method | MIR |
| Starting model (for MR) | PRD-DNA COMPLEX |
| RMSD bond length | 0.009 |
| RMSD bond angle | 21.790 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 15.000 |
| High resolution limit [Å] | 2.500 |
| Rmerge | 0.050 |
| Number of reflections | 20530 |
| Completeness [%] | 99.0 |
| Redundancy | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | pH 8.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein-DNA complex | 0.5 (mM) | |
| 10 | 1 | reservoir | EDTA | 5 (mM) | |
| 11 | 1 | reservoir | PEG200 | 20 (%) | |
| 12 | 1 | reservoir | ammonium acetate | 200 (mM) | |
| 2 | 1 | drop | HEPES | 40 (mM) | |
| 3 | 1 | drop | spermine | 10 (mM) | |
| 4 | 1 | drop | dithiothreitol | 10 (mM) | |
| 5 | 1 | drop | EDTA | 5 (mM) | |
| 6 | 1 | drop | PEG200 | 20 (%) | |
| 7 | 1 | reservoir | HEPES | 40 (mM) | |
| 8 | 1 | reservoir | spermine | 10 (mM) | |
| 9 | 1 | reservoir | dithiothreitol | 10 (mM) |
