1YRP
Catalytic domain of human ZIP kinase phosphorylated at Thr265
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, Hamburg |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-07-10 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.560, 60.930, 87.950 |
Unit cell angles | 90.00, 92.17, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.100 |
R-factor | 0.24508 |
Rwork | 0.244 |
R-free | 0.26842 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.240 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.200 |
High resolution limit [Å] | 3.100 | 3.100 |
Number of reflections | 10171 | |
<I/σ(I)> | 11.3 | 3.7 |
Completeness [%] | 97.2 | 95.5 |
Redundancy | 3.1 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 295 | PEG, MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 295K |