1E6I
Bromodomain from GCN5 complexed with acetylated H4 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-07-10 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 43.680, 71.920, 89.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.000 - 1.870 |
R-factor | 0.185 * |
Rwork | 0.187 |
R-free | 0.20900 |
Structure solution method | SIRAS |
RMSD bond length | 0.016 |
RMSD bond angle | 3.900 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHARP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.100 | 1.980 |
High resolution limit [Å] | 1.870 | 1.870 |
Rmerge | 0.073 | 0.204 |
Number of reflections | 88913 | |
<I/σ(I)> | 24.5 | 8.7 |
Completeness [%] | 99.8 | 99.5 |
Redundancy | 7.4 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 16 * | 2.2M AMMONIUM SULPHATE, 20% V/V GLYCEROL, 4MM DITHIOTHREITOL, 100 MM HEPES PH 7.5, 125MM NACL 5:1 PEPTIDE:PROTEIN |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | HEPES | 20 (mM) | |
2 | 1 | drop | 250 (mM) | ||
3 | 1 | drop | dithiothreitol | 1 (mM) | |
4 | 1 | drop | protein | 20 (mg/ml) | |
5 | 1 | reservoir | ammonium sulfate | 2.2 (M) | |
6 | 1 | reservoir | glycerol | 20 (%(v/v)) | |
7 | 1 | reservoir | dithiothreitol | 4 (mM) | |
8 | 1 | reservoir | HEPES | 100 (mM) |