6GY5
Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 297 |
| Detector technology | PIXEL |
| Collection date | 2017-09-21 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.459, 47.361, 151.933 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.650 - 1.086 |
| R-factor | 0.1543 |
| Rwork | 0.153 |
| R-free | 0.17240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vpj |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.333 |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.650 | 29.650 | 1.090 |
| High resolution limit [Å] | 1.060 | 4.740 | 1.060 |
| Rmerge | 0.071 | 0.066 | 0.448 |
| Rmeas | 0.085 | 0.077 | 0.620 |
| Rpim | 0.045 | 0.040 | 0.427 |
| Number of reflections | 130575 | 1699 | 7488 |
| <I/σ(I)> | 11.8 | 26.1 | 1.4 |
| Completeness [%] | 97.6 | 99.5 | 77.3 |
| Redundancy | 5.6 | 5.9 | 2.2 |
| CC(1/2) | 0.997 | 0.995 | 0.706 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 2M Sodium Chloride, 0.1M Acetate pH 4.5 |






