3EG6
Structure of WDR5 bound to MLL1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-01-26 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 78.254, 98.384, 80.075 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.210 - 1.720 |
| R-factor | 0.203 |
| Rwork | 0.203 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h68 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.510 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.000 | 1.780 |
| High resolution limit [Å] | 1.720 | 1.720 |
| Rmerge | 0.097 | 0.495 |
| Number of reflections | 32871 | |
| <I/σ(I)> | 23.441 | 2.6207 |
| Completeness [%] | 98.6 | 97.7 |
| Redundancy | 5.5 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 298 | 30% PEG 3350, 30 mM (NH4)2SO4, 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
