5TD7
Crystal structure of histone deacetylase 10
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL14-1 |
Synchrotron site | SSRL |
Beamline | BL14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-03-30 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 1.28211 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 80.449, 80.449, 243.037 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.506 - 2.850 |
R-factor | 0.1839 |
Rwork | 0.182 |
R-free | 0.22670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5eei |
RMSD bond length | 0.004 |
RMSD bond angle | 0.713 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.000 |
High resolution limit [Å] | 2.850 | 2.850 |
Rmerge | 0.119 | 0.930 |
Rpim | 0.070 | 0.554 |
Number of reflections | 22191 | 3182 |
<I/σ(I)> | 12.9 | 2.2 |
Completeness [%] | 99.9 | 100 |
Redundancy | 7.1 | 7.3 |
CC(1/2) | 0.997 | 0.682 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.2 M KH2PO4, 20% PEG 3350 |