1EQF
CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-09-07 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.100, 58.100, 101.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.100 - 2.100 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.24600 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.140 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MLPHARE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 51.300 | 29.100 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.079 | 0.341 |
Total number of observations | 122732 * | |
Number of reflections | 17084 | |
<I/σ(I)> | 17.3 | |
Completeness [%] | 97.0 | 97.6 |
Redundancy | 7.2 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 9.5 | 294 | ammonium sulfate, TrisCl, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 10 (mg/ml) | |
2 | 1 | 1 | ammonium sulfate | 1.4 (M) | |
3 | 1 | 1 | Tris-HCl | 100 (mM) |