1A06
CALMODULIN-DEPENDENT PROTEIN KINASE FROM RAT
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1995-09 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 65.200, 76.000, 148.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.500 |
R-factor | 0.201 |
Rwork | 0.201 |
R-free | 0.31300 |
Structure solution method | SIRAS |
RMSD bond length | 0.009 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.060 | 0.320 |
Total number of observations | 75340 * | |
Number of reflections | 12191 | |
<I/σ(I)> | 20 | 10 |
Completeness [%] | 95.0 | 89.2 * |
Redundancy | 4 | 74 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 21 * | used to seeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium salfate | 2 (M) | |
2 | 1 | reservoir | PEG400 | 2 (%(w/v)) | |
3 | 1 | reservoir | HEPES | 100 (mM) | |
4 | 1 | drop | 70 (mM) |