5LRF
Crystal structure of Glycogen Phosphorylase b in complex with KS389
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2015-09-11 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.04 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 128.560, 128.560, 116.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.140 - 1.750 |
| R-factor | 0.16628 |
| Rwork | 0.165 |
| R-free | 0.18507 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.430 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.380 | 1.840 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.050 | 0.427 |
| Number of reflections | 90698 | |
| <I/σ(I)> | 15.1 | 2.9 |
| Completeness [%] | 93.2 | 95.5 |
| Redundancy | 4.1 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | SMALL TUBES | 6.8 | 289 | 10mM BES buffer |
