4NH1
Crystal structure of a heterotetrameric CK2 holoenzyme complex carrying the Andante-mutation in CK2beta and consistent with proposed models of autoinhibition and trans-autophosphorylation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Collection date | 2012-06-12 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 210.537, 57.441, 139.394 |
| Unit cell angles | 90.00, 118.54, 90.00 |
Refinement procedure
| Resolution | 46.237 - 3.300 |
| R-factor | 0.215 |
| Rwork | 0.213 |
| R-free | 0.25140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jwh |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.632 |
| Data reduction software | XDS |
| Data scaling software | XSCALE (from XDS) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 46.240 |
| High resolution limit [Å] | 3.300 |
| Rmerge | 0.050 |
| Number of reflections | 21878 |
| <I/σ(I)> | 13.85 |
| Redundancy | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
