7D0P
Crystal structure of human HBO1-BRPF2 in complex with propionyl-coenzyme A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-04-16 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.97892 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 126.679, 39.306, 87.744 |
| Unit cell angles | 90.00, 123.01, 90.00 |
Refinement procedure
| Resolution | 50.010 - 1.800 |
| R-factor | 0.1734 |
| Rwork | 0.171 |
| R-free | 0.22560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5gk9 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.381 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.010 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 33222 | 3140 |
| <I/σ(I)> | 0.05 | 2 |
| Completeness [%] | 98.0 | |
| Redundancy | 6.5 | 5.4 |
| CC(1/2) | 1.000 | 0.950 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 0.1 M HEPES, pH 7.5, 12% w/v PEG 3350 |
