4QYL
Crystal Structure of the human BRPF1 bromodomain in complex with a histone H2AK5ac peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-04-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.075 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 60.908, 55.581, 82.135 |
| Unit cell angles | 90.00, 93.58, 90.00 |
Refinement procedure
| Resolution | 41.020 - 1.800 |
| R-factor | 0.20629 |
| Rwork | 0.204 |
| R-free | 0.25257 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3rcw |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.775 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.020 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.081 | 0.386 |
| Number of reflections | 48421 | |
| <I/σ(I)> | 21.04 | 3 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 4 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 0.2 M NH4SO4, 0.1 M MES monohydrate, pH 6.5, 30% w/v polyethylene glycol monomethyl ether (PEG) 5000, 1% propylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
