1WV1
Crystallographic studies on acyl ureas, a new class of inhibitors of glycogenphosphorylase. Broad specificity of the allosteric site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 2001-04-08 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 128.310, 128.310, 115.940 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.230 - 2.260 |
R-factor | 0.189 |
Rwork | 0.189 |
R-free | 0.23000 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.240 | 2.300 |
High resolution limit [Å] | 2.260 | 2.260 |
Rmerge | 0.129 | 0.392 |
Number of reflections | 143690 | |
<I/σ(I)> | 6.6 | 1.9 |
Completeness [%] | 94.9 | 65.7 |
Redundancy | 2.9 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | SMALL TUBES | 6.7 | 298 | 10mM Bes buffer, 3mM DDT, pH 6.7, SMALL TUBES, temperature 298K |