1KRR
Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1998-12-02 |
Detector | SIEMENS HI-STAR |
Wavelength(s) | 1.5418 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 65.700, 182.500, 121.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 26.000 - 2.500 |
R-factor | 0.193 * |
Rwork | 0.193 |
R-free | 0.24800 |
Structure solution method | MIR |
RMSD bond length | 0.011 |
RMSD bond angle | 27.000 * |
Data reduction software | X-GEN |
Data scaling software | XDS |
Phasing software | SHARP |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.089 | 0.298 |
Total number of observations | 93176 * | |
Number of reflections | 23094 | |
Completeness [%] | 90.1 | 68.8 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 298 | Wang, X.G., (1999) Acta Crystallogr., D55, 1955. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 14 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 25 (mM) | pH7.8 |
3 | 1 | drop | beta-mercaptoethanol | 1 (mM) | |
4 | 1 | drop | acetyl-CoA | 10 (mM) | |
5 | 1 | reservoir | ammonium sulfate | 2.3 (M) | |
6 | 1 | reservoir | HEPES | 0.1 (M) | pH7.4 |
7 | 1 | reservoir | L(+)-tartaric acid | 0.17 (M) |