1EAO
THE RUNX1 Runt domain at 1.4A resolution: a structural switch and specifically bound chloride ions modulate DNA binding
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-04-15 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 91.066, 46.173, 62.904 |
| Unit cell angles | 90.00, 91.94, 90.00 |
Refinement procedure
| Resolution | 24.000 * - 1.400 |
| R-factor | 0.143 |
| Rwork | 0.141 |
| R-free | 0.17200 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | EBI-8233 |
| RMSD bond length | 0.015 * |
| RMSD bond angle | 1.720 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.1.27) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.000 | 1.450 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.079 | 0.230 |
| Total number of observations | 224261 * | |
| Number of reflections | 50436 | |
| <I/σ(I)> | 10.9 | 4 |
| Completeness [%] | 97.5 | 97 * |
| Redundancy | 4.45 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | 25 % PEG 3350, 16% GLYCEROL, 130 MM NA CACODYLATE, PH 6.4 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | 1.6 (M) | ||
| 2 | 1 | drop | 100 (mM) | ||
| 3 | 1 | drop | HEPES | 20 (mM) | pH8.0 |
| 4 | 1 | drop | protein | 23 (mg/ml) | |
| 5 | 1 | reservoir | PEG3350 | 25 (%(w/v)) | |
| 6 | 1 | reservoir | glycerol | 16 (%(v/v)) | |
| 7 | 1 | reservoir | sodium cacodylate | 130 (mM) | pH6.4 |
