1FS4
Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | AREA DETECTOR |
Collection date | 1996-04-03 |
Detector | NICOLET |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 128.500, 128.500, 116.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.500 - 2.380 |
R-factor | 0.177 * |
Rwork | 0.177 |
R-free | 0.22400 * |
Structure solution method | DIFFERENCE FOURIER METHODS |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | X-GEN |
Data scaling software | XDS |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.500 | 2.490 |
High resolution limit [Å] | 2.380 | 2.380 |
Rmerge | 0.076 | |
Total number of observations | 145498 * | |
Number of reflections | 32187 * | |
Completeness [%] | 82.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 6.7 | 16 * | Oikonomakos, N.G., (1985) Biochim.Biophys.Acta., 832, 248. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | phosphorylase b | 27.5 (mg/ml) | |
2 | 1 | 1 | IMP | 1.1 (mM) | |
3 | 1 | 1 | spermine | 1.1 (mM) | |
4 | 1 | 1 | Bes | 10 (mM) | |
5 | 1 | 1 | dithiothreitol | 2.9 (mM) | |
6 | 1 | 1 | EDTA | 0.1 (mM) |