5FFV
Crystal structure of the bromodomain of human BRPF1 in complex with H3K14ac histone peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-10-13 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 74.266, 74.354, 49.509 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.730 - 1.300 |
| R-factor | 0.19077 |
| Rwork | 0.190 |
| R-free | 0.20636 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4lc2 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.333 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.730 | 1.370 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Rmerge | 0.086 | 0.425 |
| Number of reflections | 67343 | |
| <I/σ(I)> | 17.5 | 4.5 |
| Completeness [%] | 98.6 | 90.3 |
| Redundancy | 11.1 | 8.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 277.15 | 25% PEG3350, 0.2 M MgCl2, 0.1 M bis-tris pH 5.5 |
