5LRC
Crystal structure of Glycogen Phosphorylase in complex with KS114
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2015-09-09 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.0403 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 128.410, 128.410, 116.170 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.640 - 2.000 |
| R-factor | 0.16257 |
| Rwork | 0.161 |
| R-free | 0.19661 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.311 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.330 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.096 | 0.437 |
| Number of reflections | 61240 | |
| <I/σ(I)> | 8 | 3 |
| Completeness [%] | 94.1 | 96.3 |
| Redundancy | 4.2 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | SMALL TUBES | 6.8 | 289 | 10mM Bes buffer |
