3H30
Crystal structure of the catalytic subunit of human protein kinase CK2 with 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole
Replaces: 2RKPExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X12 |
Detector technology | CCD |
Collection date | 2006-09-30 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9 |
Spacegroup name | P 43 |
Unit cell lengths | 71.506, 71.506, 125.789 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.560 |
R-factor | 0.15666 |
Rwork | 0.156 |
R-free | 0.19811 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.189 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 25.000 |
High resolution limit [Å] | 1.560 |
Number of reflections | 89486 |
Completeness [%] | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 1.5M ammonium sulfate, 0.2M tri-sodium citrate, 0.2M K/Na tartrate pH 5.6, the enzyme was preincubated with 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole, VAPOR DIFFUSION, SITTING DROP, temperature 293K |