2AAT
2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI
Experimental procedure
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 156.800, 86.740, 79.840 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.800 |
| R-factor | 0.22 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.071 |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.800 * |
| Number of reflections | 8783 * |
| Completeness [%] | 64.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 7.5 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein solution | 5.2 (mg/mL) | |
| 2 | 1 | 1 | potassium phosphate | 50 (mM) | |
| 3 | 1 | 1 | ammonium sulfate | 53 (%sat) |






