1FPG
STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY
Experimental procedure
Spacegroup name | P 21 21 2 |
Unit cell lengths | 61.100, 166.500, 80.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.300 |
R-factor | 0.195 |
Rwork | 0.195 |
RMSD bond length | 0.019 |
RMSD bond angle | 1.860 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.300 * |
Rmerge | 0.074 * |
Total number of observations | 79208 * |
Number of reflections | 36031 |
Completeness [%] | 92.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 7.4 | Ke, H., (1989) J. Mol. Biol., 212, 513. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | enzyme | 5-10 (mg/ml) | |
2 | 1 | 2 | Tris base | 20 (mM) | |
3 | 1 | 2 | maleic acid | 2.5 (mM) | |
4 | 1 | 2 | EDTA | 0.1 (mM) | |
5 | 1 | 2 | 0.3 (mM) | ||
6 | 1 | 2 | PEG3350 | 4 (%(w/v)) |