3R93
Crystal structure of the chromo domain of M-phase phosphoprotein 8 bound to H3K9Me3 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-08-18 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97924 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 71.148, 74.005, 72.609 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.057 |
| R-factor | 0.222 |
| Rwork | 0.220 |
| R-free | 0.27320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lwe |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.369 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.120 |
| High resolution limit [Å] | 2.050 | 4.420 | 2.050 |
| Rmerge | 0.072 | 0.030 | 0.735 |
| Number of reflections | 24361 | ||
| <I/σ(I)> | 12.6 | ||
| Completeness [%] | 99.7 | 99.7 | 97.6 |
| Redundancy | 6.8 | 6.6 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 35% PEG2000-MME, 8-fold excess of H3K9Me3, vapor diffusion, sitting drop, temperature 293K |
