1SH5
Crystal structure of actin-binding domain of mouse plectin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X31 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-09-16 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.100 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.310, 108.920, 63.750 |
| Unit cell angles | 90.00, 115.25, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.15314 |
| Rwork | 0.151 |
| R-free | 0.19422 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qag |
| RMSD bond length | 0.027 |
| RMSD bond angle | 2.020 |
| 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] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.060 | 0.400 |
| Number of reflections | 47802 | |
| <I/σ(I)> | 22.2 | 2.1 |
| Completeness [%] | 96.2 | 71.7 |
| Redundancy | 3.5 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | PEG 8000, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
