3AAT
ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE
Experimental procedure
Spacegroup name | C 2 2 21 |
Unit cell lengths | 156.000, 87.600, 78.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.500 * |
R-factor | 0.215 |
RMSD bond length | 0.011 |
RMSD bond angle | 0.073 |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.500 * |
Rmerge | 0.067 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 50 (%sat) | |
2 | 1 | reservoir | potassium phosphate | 20 (mM) |