1SH6
Crystal structure of actin-binding domain of mouse plectin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-10-02 |
Detector | MARRESEARCH |
Wavelength(s) | 0.8120 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 32.517, 51.226, 144.717 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.20238 |
Rwork | 0.198 |
R-free | 0.29956 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.037 |
RMSD bond angle | 2.594 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.020 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.038 | 0.310 |
Number of reflections | 17114 | |
<I/σ(I)> | 33.9 | 3.5 |
Completeness [%] | 97.6 | 86.3 |
Redundancy | 5.1 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | PEG 8000, cacodylate, calcium acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |