1YR5
1.7-A structure of calmodulin bound to a peptide from DAP kinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-01-30 |
Detector | MARRESEARCH |
Wavelength(s) | 0.938 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 66.070, 33.710, 75.890 |
Unit cell angles | 90.00, 111.16, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.700 |
R-factor | 0.20286 |
Rwork | 0.200 |
R-free | 0.25707 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wrz |
RMSD bond length | 0.015 |
RMSD bond angle | 1.442 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.750 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 16769 | |
<I/σ(I)> | 20.1 | 2.6 |
Completeness [%] | 96.8 | 94.5 |
Redundancy | 4.6 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 295 | PEG 8000, sodium acetate, calcium chloride, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K |