5DC6
Crystal structure of D176N-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 | 82.332, 98.206, 104.281 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.103 - 1.553 |
R-factor | 0.1477 |
Rwork | 0.147 |
R-free | 0.16630 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ewf |
RMSD bond length | 0.010 |
RMSD bond angle | 1.246 |
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] | 49.103 | 1.610 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.110 | 1.039 |
Number of reflections | 122036 | |
<I/σ(I)> | 15.6 | 2 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 7.1 | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 100 mM Tris (pH 8.0), 13% (w/v) PEG 8000, and 4 mM TCEP |