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 |