1BSX
STRUCTURE AND SPECIFICITY OF NUCLEAR RECEPTOR-COACTIVATOR INTERACTIONS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 105 |
Detector technology | IMAGE PLATE |
Collection date | 1997-11-15 |
Detector | RIGAKU |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 95.200, 95.200, 137.600 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 100.000 - 3.700 |
R-factor | 0.249 |
Rwork | 0.249 |
R-free | 0.29900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HUMAN THYROID HORMONE RECEPTOR BETA |
RMSD bond length | 0.010 * |
RMSD bond angle | 1.600 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 3.660 |
High resolution limit [Å] | 3.600 | 3.600 |
Rmerge | 0.077 | 0.261 |
Total number of observations | 35565 * | |
Number of reflections | 8490 | 411 * |
<I/σ(I)> | 12 | 3.7 |
Completeness [%] | 96.3 | 96.3 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.9 | 4 * | pH 4.9 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | peptide | ||
2 | 1 | drop | PEG4000 | 15 (%) | |
3 | 1 | drop | sodium citrate | 200 (mM) | |
4 | 1 | reservoir | PEG4000 | 10 (%) | |
5 | 1 | reservoir | ammonium acetate | 100 (mM) | |
6 | 1 | reservoir | sodium citrate | 50 (mM) |