6OI3
Crystal structure of human WDR5 in complex with monomethyl H3R2 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-06-28 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.97931 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 78.294, 98.632, 80.265 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 61.320 - 1.660 |
| R-factor | 0.1731 |
| Rwork | 0.172 |
| R-free | 0.20180 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h14 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.453 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 61.320 | 1.690 |
| High resolution limit [Å] | 1.660 | 1.660 |
| Rpim | 0.070 | 0.340 |
| Number of reflections | 37045 | 1856 |
| <I/σ(I)> | 8.2 | 2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.1 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.9 | 295 | 100 mM Bis-Tris pH 5.9, 32% PEG3350, 54.6 mM Ammonium Sulfate, 1.67 mM monomethyl H3R2 peptide |
