1KHU
Smad1 crystal structure reveals the details of BMP signaling pathway
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 113 |
Spacegroup name | H 3 |
Unit cell lengths | 138.129, 138.129, 199.340 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.000 - 2.500 |
R-factor | 0.239 * |
Rwork | 0.239 |
R-free | 0.27400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Smad4 active fragment homotrimer |
RMSD bond length | 0.008 |
RMSD bond angle | 1.397 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.570 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.065 | 0.351 * |
Total number of observations | 77509 * | |
Number of reflections | 47621 | |
<I/σ(I)> | 10.4 | 2 |
Completeness [%] | 96.8 * | 98.8 |
Redundancy | 1.69 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 * | 298 | alcohol, pH 6.5, EVAPORATION, temperature 298.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | MES | 50 (mM) | pH6.0 |
2 | 1 | reservoir | ethanol | 6 (%) | |
3 | 1 | drop | protein | 20 (mg/ml) |