4HE0
Crystal structure of human muscle fructose-1,6-bisphosphatase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-12-15 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.5418 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 73.853, 73.853, 146.749 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.690 |
R-factor | 0.202 |
Rwork | 0.200 |
R-free | 0.25280 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1eyi |
RMSD bond length | 0.012 |
RMSD bond angle | 1.393 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.790 |
High resolution limit [Å] | 2.690 | 5.790 | 2.690 |
Rmerge | 0.184 | 0.083 | 0.509 |
Number of reflections | 11946 | ||
<I/σ(I)> | 6.6 | ||
Completeness [%] | 99.9 | 98.9 | 100 |
Redundancy | 8.8 | 8.5 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 0.1M MgCl2, 15% PEG 4000, 0.1M Hepes pH 7.5, vapor diffusion, hanging drop, temperature 295K |