5EFN
Crystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 (H574A) in complex with histone H4 Lys6 tripeptide substrate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-08-13 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00003 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.997, 83.908, 86.903 |
| Unit cell angles | 90.00, 98.12, 90.00 |
Refinement procedure
| Resolution | 12.338 - 1.804 |
| R-factor | 0.1638 |
| Rwork | 0.162 |
| R-free | 0.19410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5eek |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.041 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.3_1479) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.950 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.142 | 0.713 |
| Number of reflections | 70941 | |
| <I/σ(I)> | 9.9 | 1.8 |
| Completeness [%] | 98.9 | 99.9 |
| Redundancy | 3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 0.1 M Bis-Tris, pH 6.5, 25% PEG3350 |
