5YBV
The structure of the KANK2 ankyrin domain with the 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 | 2017-01-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9796 |
| Spacegroup name | P 1 |
| Unit cell lengths | 45.956, 52.834, 53.478 |
| Unit cell angles | 73.02, 89.67, 84.91 |
Refinement procedure
| Resolution | 34.467 - 2.120 |
| R-factor | 0.192 |
| Rwork | 0.188 |
| R-free | 0.23500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hbd |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.277 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (dev_2722) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 34.470 |
| High resolution limit [Å] | 2.120 |
| Number of reflections | 25270 |
| <I/σ(I)> | 10.2 |
| Completeness [%] | 92.9 |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 0.1M HEPES (pH7.5), 0.15M ammonium acetate, 31 % PEG 3350 |
