1Q1A
Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-02-20 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9 |
Spacegroup name | H 3 |
Unit cell lengths | 98.421, 98.421, 77.254 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.740 - 1.500 |
R-factor | 0.183 |
Rwork | 0.183 |
R-free | 0.20900 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1q14 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.220 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.049 | 0.172 |
Number of reflections | 43331 * | |
<I/σ(I)> | 20.9 | 4.2 |
Completeness [%] | 96.9 | 93.9 |
Redundancy | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 294 | PEG 4K, , pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | 0.2 (M) | ||
3 | 1 | reservoir | sodium citrate | 100 (mM) | pH5.6 |
4 | 1 | reservoir | PEG4000 | 25 (%) |