1CG3
STRUCTURE OF THE MUTANT (R143L) 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 | 80.940, 80.940, 158.180 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 5.000 - 2.500 |
R-factor | 0.157 * |
Rwork | 0.162 |
R-free | 0.24000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gim |
RMSD bond length | 0.012 |
RMSD bond angle | 1.890 |
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 | 0.091 | |
Total number of observations | 165859 * | |
Number of reflections | 26553 | |
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 | 13 (%(w/w)) | |
9 | 1 | reservoir | magnesium chloride | 200 (mM) |