1LPU
Low Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR571 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-08-20 |
Detector | MACSCIENCE |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 143.190, 59.758, 45.082 |
Unit cell angles | 90.00, 103.41, 90.00 |
Refinement procedure
Resolution | 69.000 * - 1.860 |
R-factor | 0.204 * |
Rwork | 0.204 |
R-free | 0.24800 * |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 1a6o |
RMSD bond length | 0.016 |
RMSD bond angle | 1.438 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 69.000 * | 1.920 |
High resolution limit [Å] | 1.860 | 1.860 |
Rmerge | 0.084 * | 0.473 * |
Number of reflections | 31230 | |
<I/σ(I)> | 28.4 | 4 |
Completeness [%] | 99.6 * | 89.8 |
Redundancy | 8.8 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.1 | 20 * | used microseeding * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG3350 | 20 (%(w/v)) | |
2 | 1 | reservoir | sodium acetate | 200 (mM) | |
3 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.1 |