7D0S
Crystal structure of human HBO1-BRPF2 in complex with succinyl-coenzyme A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-12-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 127.098, 39.565, 88.328 |
| Unit cell angles | 90.00, 122.88, 90.00 |
Refinement procedure
| Resolution | 50.010 - 2.300 |
| R-factor | 0.2155 |
| Rwork | 0.213 |
| R-free | 0.25650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5gk9 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.440 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.010 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.100 | 0.770 |
| Number of reflections | 16040 | 1280 |
| <I/σ(I)> | 23.3 | 2.7 |
| Completeness [%] | 94.7 | |
| Redundancy | 5.8 | 3.6 |
| CC(1/2) | 1.000 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 0.2 M L-Proline, 0.1 M HEPES, pH 7.5, 24% w/v PEG 1500 |
