9MXA
Crystal structure of the DNA binding domain of FLI1 (wild-type) in complex with a DNA containing two contiguous GGAA sites
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 | PIXEL |
| Collection date | 2020-12-01 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | I 41 2 2 |
| Unit cell lengths | 96.949, 96.949, 185.748 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.590 |
| R-factor | 0.26179 |
| Rwork | 0.260 |
| R-free | 0.28738 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5jvt |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.376 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.630 |
| High resolution limit [Å] | 2.590 | 2.590 |
| Rmerge | 0.071 | |
| Number of reflections | 13984 | 699 |
| <I/σ(I)> | 47 | |
| Completeness [%] | 98.9 | |
| Redundancy | 13.6 | |
| CC(1/2) | 1.000 | 0.899 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 294 | 0.1 M Tris, pH 8.5, 2 M ammonium phosphate |
