3BZI
Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization
Replaces: 2OJSExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.726, 67.481, 87.888 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.840 - 2.100 |
| R-factor | 0.17785 |
| Rwork | 0.174 |
| R-free | 0.24579 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1owl |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.959 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 36.840 |
| High resolution limit [Å] | 2.100 |
| Number of reflections | 12144 |
| Completeness [%] | 90.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 298 | 100mM HEPES pH 7.5, 2M ammonium formate, VAPOR DIFFUSION, temperature 298K |
