1QM5
Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 107.410, 61.500, 132.380 |
Unit cell angles | 90.00, 105.03, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.228 |
Rwork | 0.228 |
R-free | 0.26100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.102 | |
Total number of observations | 152192 * | |
Number of reflections | 72681 | |
Completeness [%] | 80.0 | 64.5 |
Redundancy | 2.1 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | (26-32)% PEG 4000, (0.1-0.6)M LICL, 0.1M TRIS/HCL PH8.5, 18 DEG C, HANGING DROP, 10MG/ML PROTEIN, 20MM GSG4, 50MM PHOSPHATE, pH 8.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | GSG4 | ||
3 | 1 | drop | 50 (mM) | ||
4 | 1 | reservoir | PEG4000 | 26-32 (%) | |
5 | 1 | reservoir | 0.1-0.6 (M) | ||
6 | 1 | reservoir | Tris-HCl | 1 (M) |