2C4M
Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-03-16 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 99.266, 187.620, 129.315 |
Unit cell angles | 90.00, 112.48, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.216 |
Rwork | 0.216 |
R-free | 0.23200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gpa |
RMSD bond length | 0.011 |
RMSD bond angle | 1.500 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.080 | 0.240 |
Number of reflections | 306185 | |
<I/σ(I)> | 5.1 | 3.1 |
Completeness [%] | 89.7 | 75.9 |
Redundancy | 2.6 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | HANGING DROP VAPOUR DIFFUSION 8.4MG/ML PROTEIN SOLUTION, 0.1M SODIUM ACETATE PH 5.0, 8% PEG 8,000, 0.2M SODIUM FORMATE |