1ASM
CRYSTAL STRUCTURES OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE IN TWO CONFORMATIONS: COMPARISON OF AN UNLIGANDED OPEN AND TWO LIGANDED CLOSED FORMS
Experimental procedure
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 85.400, 78.800, 89.600 |
| Unit cell angles | 90.00, 118.60, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.350 |
| R-factor | 0.1878 |
| Rwork | 0.188 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.271 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.350 * |
| Rmerge | 0.044 * |
| Number of reflections | 39857 * |
| Completeness [%] | 91.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | referred to 'Smith, D. L.', (1986) J. Mol. Biol., 191, 301-302 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | reservoir | sodium phosphate | 0.025 (M) | |
| 3 | 1 | reservoir | PLP | 0.02 (mM) | |
| 4 | 1 | reservoir | ammonium sulfate | 50 (%sat) |






