4QSQ
Structure of the bromodomain of human ATPase family AAA domain-containing protein 2 (ATAD2) with bound DMSO
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2011-12-06 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 79.248, 79.248, 138.189 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.120 - 1.800 |
R-factor | 0.15974 |
Rwork | 0.158 |
R-free | 0.19366 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | pdb id: 3DAI |
RMSD bond length | 0.016 |
RMSD bond angle | 1.606 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.910 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.119 | 0.842 |
Number of reflections | 24039 | |
<I/σ(I)> | 9.4 | 2 |
Completeness [%] | 98.5 | 98.1 |
Redundancy | 5.6 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 277.15 | apo crystals grew in 1.8-2.2 M ammonium sulphate, 0.1 M Bis-Tris, pH 5.5-6.5. Soaking performed in 28-32% PEG 3350, 50 mM bis-tris pH 5.5, 50 mM ammonium phosphate and 20% ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K |