5E8I
Crystal structure of the DNA binding domain of human transcription factor FLI1 in complex with a 10-mer DNA ACCGGAAGTG
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-08-05 |
| Detector | RAYONIX MX300HS |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 86.647, 86.647, 230.282 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.000 - 3.450 |
| R-factor | 0.22482 |
| Rwork | 0.222 |
| R-free | 0.27142 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4iri |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.878 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.510 |
| High resolution limit [Å] | 3.450 | 3.450 |
| Rmerge | 0.100 | 0.870 |
| Number of reflections | 13800 | |
| <I/σ(I)> | 19 | 1.9 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 8.2 | 7.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 294 | 0.1 M Na cacodylate pH 6.5, 0.2 M CaCl2, 14% w/v PEG 8000 |
