8XV8
Crystal structure of PHD domain of UHRF1 in complex with hStella peptide (residues 75-121)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-04-01 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9785 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.029, 46.020, 82.910 |
| Unit cell angles | 90.00, 112.76, 90.00 |
Refinement procedure
| Resolution | 38.230 - 2.050 |
| R-factor | 0.18728 |
| Rwork | 0.186 |
| R-free | 0.20730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3shb |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.740 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.230 | 2.110 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.098 | 0.656 |
| Rmeas | 0.108 | 0.749 |
| Rpim | 0.044 | 0.348 |
| Total number of observations | 164753 | 8590 |
| Number of reflections | 28518 | 1941 |
| <I/σ(I)> | 10.4 | 2.4 |
| Completeness [%] | 97.9 | |
| Redundancy | 5.8 | 4.4 |
| CC(1/2) | 0.991 | 0.800 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | 0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 |
