1T5C
Crystal structure of the motor domain of human kinetochore protein CENP-E
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-08-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.933 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.353, 83.700, 94.162 |
Unit cell angles | 90.00, 103.05, 90.00 |
Refinement procedure
Resolution | 12.000 - 2.500 |
Rwork | 0.228 |
R-free | 0.27820 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Structure of conventional kinesin motor domain PDB entry 1MKJ |
RMSD bond length | 0.012 |
RMSD bond angle | 2.080 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 91.730 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.072 | 0.182 |
Number of reflections | 25345 | |
<I/σ(I)> | 6.4 | 4.4 |
Completeness [%] | 97.7 | 86.1 |
Redundancy | 4.7 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7 | 292 | PEG 3350, NaNO3, Pipes, pH 7.0, VAPOR DIFFUSION, temperature 292K |