1PJK
Crystal Structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 283 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-12-06 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 59.044, 46.502, 64.262 |
| Unit cell angles | 90.00, 112.02, 90.00 |
Refinement procedure
| Resolution | 17.300 - 2.500 |
| R-factor | 0.18792 |
| Rwork | 0.180 |
| R-free | 0.25700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | CHAIN A of PDB ENTRY 1JWH |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.120 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.300 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.118 * | 0.602 * |
| Number of reflections | 11207 | 1136 * |
| <I/σ(I)> | 8.4 | |
| Completeness [%] | 98.5 | 99.9 |
| Redundancy | 2.3 | 2.3 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 20 * | PEGmme 5000, ammonium sulfate, MES, adenylyl imidodiphosphate, magnesium chloride, peptide RRRADDSDDDDD, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG5000 MME | 30 (%(w/v)) | |
| 2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 3 | 1 | reservoir | MES | 0.1 (M) | pH7.5 |
| 4 | 1 | drop | 2 (mM) | ||
| 5 | 1 | drop | AMP-PNP | 1 (mM) | |
| 6 | 1 | drop | peptide | 0.62 (mM) |
