1AAW
THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI
Experimental procedure
Spacegroup name | C 2 2 21 |
Unit cell lengths | 156.800, 86.900, 80.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 5.000 * - 2.400 |
R-factor | 0.208 |
RMSD bond length | 0.016 |
RMSD bond angle | 6.000 |
Phasing software | X-PLOR |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.400 * |
Number of reflections | 15069 * |
Completeness [%] | 72.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 * | referred to J.Mol.Biol. 191.301-302 1986 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | drop | sodium phosphate | 0.025 (M) | |
3 | 1 | drop | PLP | 0.02 (mM) | |
4 | 1 | drop | ammonium sulfate | 50 (%sat) |