2F2O
Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X8C |
| Synchrotron site | NSLS |
| Beamline | X8C |
| Temperature [K] | 100 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 121.237, 42.769, 71.150 |
| Unit cell angles | 90.00, 110.39, 90.00 |
Refinement procedure
| Resolution | 67.420 - 2.170 |
| R-factor | 0.21235 |
| Rwork | 0.204 |
| R-free | 0.28856 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2f2p |
| RMSD bond length | 0.048 |
| RMSD bond angle | 3.065 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 67.420 |
| High resolution limit [Å] | 2.170 |
| Number of reflections | 18574 |
| Completeness [%] | 97.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | VAPOR DIFFUSION, HANGING DROP, temperature 298K |
