6KZU
Macrocyclization of an all-D linear peptide improves target affinity and imparts cellular activity: A novel stapled alpha-helical peptide modality
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-10-01 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.95370 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 82.567, 82.567, 54.783 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.490 - 1.790 |
| R-factor | 0.2027 |
| Rwork | 0.199 |
| R-free | 0.23610 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4umn |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.562 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.900 | 1.820 |
| High resolution limit [Å] | 1.790 | 1.790 |
| Rmerge | 0.065 | 1.745 |
| Rpim | 0.390 | |
| Number of reflections | 10913 | 599 |
| <I/σ(I)> | 25.6 | 1.6 |
| Completeness [%] | 100.0 | |
| Redundancy | 20.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 289 | 800 mM Sodium di-hydrogen phosphate, 800 mM di-Potassium hydrogen phosphate, 100 mM HEPES pH 7.5 |
