5D1D
Crystal structure of P91L-Y306F HDAC8 in complex with a tetrapeptide substrate
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 | 2014-02-23 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.075 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 82.281, 97.987, 105.933 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.500 - 2.011 |
| R-factor | 0.1765 |
| Rwork | 0.175 |
| R-free | 0.20640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ewf |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.722 |
| 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] | 44.500 | 2.080 |
| High resolution limit [Å] | 2.010 | 2.010 |
| Rmerge | 0.135 | 1.153 |
| Number of reflections | 57560 | |
| <I/σ(I)> | 13.2 | 2.1 |
| Completeness [%] | 99.9 | 98.8 |
| Redundancy | 9.5 | 9.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 294 | 100 mM Tris (pH 8.0), 10% (w/v) PEG 35000, 4 mM TCEP |
