3T92
Crystal structure of the Taz2:C/EBPepsilon-TAD chimera protein
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 | 2010-06-20 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.000 |
Spacegroup name | P 65 |
Unit cell lengths | 47.860, 47.860, 104.130 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 1.500 |
R-factor | 0.18024 |
Rwork | 0.178 |
R-free | 0.22790 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.310 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MrBUMP |
Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.600 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.070 | 0.440 |
Number of reflections | 20897 | |
<I/σ(I)> | 11.4 | 2.9 |
Completeness [%] | 96.8 | 98.7 |
Redundancy | 4.4 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Micro batch under oil | 8.5 | 277 | 200mM NaCl, 5mM TCEP and 20% isopropanol, pH 8.5, Micro batch under oil, temperature 277K |