4AMG
Crystal structure of the glycosyltransferase SnogD from Streptomyces nogalater
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 66.676, 179.798, 70.246 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 60.000 - 2.590 |
| R-factor | 0.22177 |
| Rwork | 0.221 |
| R-free | 0.24258 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4amb |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.321 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0119) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.300 | 2.730 |
| High resolution limit [Å] | 2.590 | 2.590 |
| Rmerge | 0.060 | 0.350 |
| Number of reflections | 26051 | |
| <I/σ(I)> | 15.2 | 2 |
| Completeness [%] | 96.2 | 82.4 |
| Redundancy | 3 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.7 | 16 % (W/V) PEG 3350, 0.2 M MGCL2, 0.1 M BISTRIS PH 5.7 |
