1DD1
CRYSTAL STRUCTURE ANALYSIS OF THE SMAD4 ACTIVE FRAGMENT
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Detector technology | IMAGE PLATE |
Collection date | 1999-06-16 |
Detector | RIGAKU |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 142.433, 142.433, 195.478 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 2.620 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.17500 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.207 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.680 |
High resolution limit [Å] | 2.620 | 2.620 |
Rmerge | 0.143 | 0.020 |
Number of reflections | 29751 | |
<I/σ(I)> | 11.17 | |
Completeness [%] | 92.9 | 96.3 |
Redundancy | 5.02 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | drop was combined with an equal volume of reservoir solution * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 40 (mg/ml) | |
2 | 1 | reservoir | HEPES | 100 (mM) | |
3 | 1 | reservoir | PEG4000 | 10 (%) | |
4 | 1 | reservoir | 200 (mM) |