2O5G
Calmodulin-smooth muscle light chain kinase peptide complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-06-06 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 28.861, 56.894, 44.760 |
| Unit cell angles | 90.00, 97.45, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.080 |
| R-factor | 0.14351 |
| Rwork | 0.142 |
| R-free | 0.16480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.799 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.796 | 1.140 |
| High resolution limit [Å] | 1.080 | 1.080 |
| Number of reflections | 61087 | |
| <I/σ(I)> | 11.2 | 2.1 |
| Redundancy | 2.8 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 30% PEG 400, 0.2 M sodium acetate, 0.1 M Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
