1CM1
MOTIONS OF CALMODULIN-SINGLE-CONFORMER REFINEMENT
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F2 |
Synchrotron site | CHESS |
Beamline | F2 |
Temperature [K] | 302 |
Detector technology | CCD |
Collection date | 1996-05 |
Detector | PRINCETON 2K |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 38.751, 75.209, 120.073 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.000 |
R-factor | 0.234 |
Rwork | 0.234 |
R-free | 0.30200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 1CDM AND 1CDL |
RMSD bond length | 0.009 |
RMSD bond angle | 21.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 11522 | |
<I/σ(I)> | 9.2 | |
Completeness [%] | 92.1 | 82.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.2 | used to seeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | sodium acetate | 100 (mM) | |
2 | 1 | reservoir | PEG6000 | 20 (%) | |
3 | 1 | reservoir | 10 (mM) | ||
4 | 1 | reservoir | sodium azide | 0.02 (%) | |
5 | 1 | drop | bovine | 14 (mg/ml) | |
6 | 1 | drop | peptide | 4 (mg/ml) | |
7 | 1 | drop | PEG6000 | 4.3 (%) |