1CG1
STRUCTURE OF THE MUTANT (K16Q) OF ADENYLOSUCCINATE SYNTHETASE FROM E. COLI COMPLEXED WITH HADACIDIN, GDP, 6-PHOSPHORYL-IMP, AND MG2+
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | SIEMENS |
| Temperature [K] | 120 |
| Detector technology | AREA DETECTOR |
| Collection date | 1997-05 |
| Detector | SIEMENS |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 80.370, 80.370, 158.520 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 5.000 - 2.500 |
| R-factor | 0.169 * |
| Rwork | 0.169 |
| R-free | 0.24900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gim |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.970 |
| Data reduction software | X-GEN |
| Data scaling software | X-GEN |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.700 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.074 | |
| Total number of observations | 178309 * | |
| Number of reflections | 27094 | |
| Completeness [%] | 99.0 | 99 |
| Redundancy | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | drop consists of equal volume of enzyme and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | imidazole | 50 (mM) | |
| 2 | 1 | drop | succinate | 75 (mM) | |
| 3 | 1 | drop | GTP | 4 (mM) | |
| 4 | 1 | drop | IMP | 4 (mM) | |
| 5 | 1 | drop | hadacidin | 5 (mM) | |
| 6 | 1 | drop | protein | 10 (mg/ml) | |
| 7 | 1 | reservoir | PEG8000 | 13 (%(w/w)) | |
| 8 | 1 | reservoir | cacodylic acid/cacodylate | 100 (mM) | |
| 9 | 1 | reservoir | magnesium chloride | 200 (mM) |
