1AKC
Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking its pyridoxal-5'-phosphate-binding lysine residue
Experimental procedure
Spacegroup name | C 2 2 21 |
Unit cell lengths | 69.800, 91.300, 127.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.300 |
R-factor | 0.172 |
RMSD bond length | 0.011 |
RMSD bond angle | 0.042 |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 10.000 * |
High resolution limit [Å] | 2.300 * |
Rmerge | 0.075 * |
Total number of observations | 38502 * |
Number of reflections | 16434 * |
Completeness [%] | 88.6 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | other * | 7.5 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
2 | 1 | drop | PEG | 9-14 (%) | |
3 | 1 | drop | sodium phosphate | 20 (mM) | |
4 | 1 | drop | 0.9 (M) | ||
5 | 1 | drop | PPxy-Glu | 20 (mM) | |
6 | 1 | drop | apoenzyme | 10 (mg/ml) | |
7 | 1 | reservoir | PEG | 18-28 (%) | |
8 | 1 | reservoir | sodium phosphate | 20 (mM) |