1MF1
Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with AMP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 70.240, 70.240, 199.140 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.700 |
| Rwork | 0.219 |
| R-free | 0.26500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 23.000 * |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.700 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.062 * | 0.330 * |
| Total number of observations | 152538 * | |
| Number of reflections | 14742 | |
| <I/σ(I)> | 7.5 | |
| Completeness [%] | 99.5 | 99.9 |
| Redundancy | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | PEG, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 10 | 1 | reservoir | magnesium acetate | 200 (mM) | |
| 2 | 1 | drop | HEPES | 50 (mM) | pH7. |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | drop | dithiothreitol | 1 (mM) | |
| 5 | 1 | drop | EDTA | 0.5 (mM) | |
| 6 | 1 | drop | AMP | 10 (mM) | |
| 7 | 1 | drop | magnesium acetate | 10 (mM) | |
| 8 | 1 | reservoir | HEPES | 100 (mM) | pH7. |
| 9 | 1 | reservoir | PEG8000 |
