1ADO
FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE
Experimental procedure
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Collection date | 1991-10 |
| Detector | SIEMENS |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 163.880, 57.470, 85.030 |
| Unit cell angles | 90.00, 102.70, 90.00 |
Refinement procedure
| Resolution | 12.000 - 1.900 |
| R-factor | 0.162 |
| Rwork | 0.162 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | STRUCTURE TO 2.7 ANGSTROM RESOLUTION |
| RMSD bond length | 0.007 |
| RMSD bond angle | 21.890 * |
| Data reduction software | X-GEN |
| Data scaling software | X-GEN |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 12.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.056 * | 0.286 * |
| Number of reflections | 103662 | |
| <I/σ(I)> | 14.5 | 1.9 |
| Completeness [%] | 85.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.3 * | Eagles, P. A., (1969) J. Mol. Biol., 45, 533-544 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 5 (mg/ml) | |
| 2 | 1 | 1 | triethanolamine-hydrochloride | 0.1 (M) | |
| 3 | 1 | 1 | EDTA | 5 (mM) | |
| 4 | 1 | 1 | ammonium sulfate | 44-49 (%sat) |
