1AA2
CALPONIN HOMOLOGY (CH) DOMAIN FROM HUMAN BETA-SPECTRIN
Experimental procedure
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR571 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-02 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 31.471, 53.685, 32.197 |
Unit cell angles | 90.00, 106.25, 90.00 |
Refinement procedure
Resolution | 14.000 - 2.000 |
R-factor | 0.16 |
R-free | 0.21300 * |
Structure solution method | MIR |
RMSD bond length | 0.019 |
RMSD bond angle | 2.059 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASES |
Refinement software | TNT (5E) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 14.000 | 2.040 |
High resolution limit [Å] | 2.000 | 2.010 |
Rmerge | 0.074 | 0.265 |
Total number of observations | 27400 * | |
Number of reflections | 6859 | |
<I/σ(I)> | 12 | 3 |
Completeness [%] | 99.1 | 97.2 |
Redundancy | 5.5 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.6 | 20 * | PROTEIN WAS CRYSTALLIZED FROM 30% PEG 8000, 100 MM SODIUM CACODYLATE, PH 6.6 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | CH domain | 10 (mg/ml) | |
2 | 1 | drop | sodium phosphate | 20 (mM) | |
3 | 1 | drop | 25 (mM) | ||
4 | 1 | drop | dithiothreitol | 1 (mM) | |
5 | 1 | drop | 1 (mM) | ||
6 | 1 | reservoir | sodium cacodylate | 0.1 (M) | |
7 | 1 | reservoir | sodium acetate | 0.2 (M) | |
8 | 1 | reservoir | PEG8000 | 30 (%(w/v)) |