5T1G
chromo shadow domain of CBX1 in complex with a histone 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 | 2013-12-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9791827 |
| Spacegroup name | F 2 2 2 |
| Unit cell lengths | 69.657, 76.887, 78.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.070 - 1.900 |
| R-factor | 0.2156 |
| Rwork | 0.213 |
| R-free | 0.24310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fmm |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.480 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.27) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 43.070 | 43.070 | 1.840 |
| High resolution limit [Å] | 1.800 | 9.000 | 1.800 |
| Rmerge | 0.075 | 0.028 | 1.478 |
| Rmeas | 0.081 | 0.031 | 1.596 |
| Rpim | 0.030 | 0.013 | 0.596 |
| Total number of observations | 71509 | 525 | 3905 |
| Number of reflections | 9891 | ||
| <I/σ(I)> | 16.9 | 56.9 | 1.3 |
| Completeness [%] | 99.9 | 97 | 99.4 |
| Redundancy | 7.2 | 5.6 | 6.9 |
| CC(1/2) | 0.999 | 0.997 | 0.788 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 1.5 M sodium citrate, 0.1 M HEPES |
