1MJB
Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 93 |
Detector technology | IMAGE PLATE |
Collection date | 2001-08-11 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | I 41 3 2 |
Unit cell lengths | 181.783, 181.783, 181.783 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.232 |
Rwork | 0.229 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fy7 |
RMSD bond length | 0.006 * |
RMSD bond angle | 1.222 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.056 | 0.291 |
Total number of observations | 162442 * | |
Number of reflections | 18056 * | |
<I/σ(I)> | 13.6 | 3 |
Completeness [%] | 97.0 | 96.4 |
Redundancy | 9.3 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 20 * | sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 0.2 (mM) | |
2 | 1 | drop | Ac-CoA | 0.5 (mM) | |
3 | 1 | reservoir | sodium cacodylate | 100 (mM) | pH6.5 |
4 | 1 | reservoir | ammonium sulfate | 1.5-1.7 (M) |