5E8G
Crystal structure of the DNA binding domain of human transcription factor FLI1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-05-29 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.978 |
Spacegroup name | H 3 |
Unit cell lengths | 140.551, 140.551, 85.140 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.000 - 2.700 |
R-factor | 0.19896 |
Rwork | 0.196 |
R-free | 0.24835 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4irg |
RMSD bond length | 0.009 |
RMSD bond angle | 1.233 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.750 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.090 | 0.670 |
Number of reflections | 17449 | |
<I/σ(I)> | 27 | 2.3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4.6 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 294 | 0.1 M sodium acetate pH 5.5, 0.1 M Co2+ sulfate heptahydrate, 24% PEG 4000 |