1MB8
Crystal Structure of the actin binding domain of plectin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-07-24 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 33.597, 79.283, 82.370 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.000 * - 2.150 |
Rwork | 0.212 |
R-free | 0.26100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS (1.1) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 32.000 * | 2.280 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.082 * | 0.319 * |
Total number of observations | 42883 * | |
Number of reflections | 11486 | |
Completeness [%] | 91.2 * | 61.4 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Tris | 0.1 (M) | pH7.0 |
2 | 1 | reservoir | 2-propanol | 15 (%(v/v)) | |
3 | 1 | drop | protein | 20 (mg/ml) | |
4 | 1 | drop | Tris | 20 (mM) | pH7.0 |
5 | 1 | drop | 150 (mM) |