5DC8
Crystal structure of H142A-Y306F HDAC8 in complex with a tetrapeptide substrate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-02-20 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 82.800, 97.887, 104.612 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.000 - 1.300 |
| R-factor | 0.1293 |
| Rwork | 0.128 |
| R-free | 0.14890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ewf |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.260 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_1833) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.000 | 1.350 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Rmerge | 0.090 | 0.855 |
| Number of reflections | 208317 | |
| <I/σ(I)> | 17.8 | 2.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 100 mM Tris (pH 8.0), 10% (w/v) PEG 35000, and 4 mM TCEP |
