5YBU
Structure of the KANK1 ankyrin domain in complex with KIF21A peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U1 |
| Synchrotron site | SSRF |
| Beamline | BL17U1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-01-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9796 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.648, 51.624, 137.609 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.335 - 1.890 |
| R-factor | 0.2249 |
| Rwork | 0.222 |
| R-free | 0.25290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hbd |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.227 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (dev_2722) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 48.335 |
| High resolution limit [Å] | 1.890 |
| Number of reflections | 22149 |
| <I/σ(I)> | 29.3 |
| Completeness [%] | 99.5 |
| Redundancy | 13.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.05M magnesium formate, 21% PEG 3350 |






