1DCH
CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR
Experimental procedure
Temperature [K] | 293 |
Collection date | 1994-05-26 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 105.650, 105.650, 196.230 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 6.000 - 3.000 |
R-factor | 0.184 |
RMSD bond length | 0.019 |
RMSD bond angle | 2.900 |
Refinement software | TNT |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 * |
High resolution limit [Å] | 3.000 * |
Rmerge | 0.060 |
Total number of observations | 86670 * |
Number of reflections | 21436 * |
Completeness [%] | 82.2 * |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.2 | 20 * | pH 7.2 COMPND ROOM TEMP., 1.7M AMSO4, .1M HEPES, PH 7.2. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 15-20 (mg/ml) | |
2 | 1 | 2 | 5 (mM) | ||
3 | 1 | 2 | methionine | 5 (mM) | |
4 | 1 | 2 | ammonium sulfate | 1.2 (M) | |
5 | 1 | 2 | PEG400 | 2 (%) | |
6 | 1 | 2 | HEPES | 0.1 (M) |