1LR4
Room Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays
Replaces: 1A6OExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
| Synchrotron site | MPG/DESY, HAMBURG |
| Beamline | BW6 |
| Temperature [K] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-10-02 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 142.550, 61.440, 45.410 |
| Unit cell angles | 90.00, 103.06, 90.00 |
Refinement procedure
| Resolution | 26.000 - 2.000 |
| R-factor | 0.193 * |
| Rwork | 0.193 |
| R-free | 0.23700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | BACKBONE OF CYCLIN-DEPENDENT KINASE 2 (PDB entry 1HCL) |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.520 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | X-PLOR |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.000 * | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.106 * | 0.111 * |
| Number of reflections | 24342 | |
| Completeness [%] | 93.7 * | 84.9 |
| Redundancy | 2.8 | 1.7 |
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 |






