6IDV
Peptide Asparaginyl Ligases from Viola yedoensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-07-04 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.953723 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 156.800, 69.800, 104.480 |
| Unit cell angles | 90.00, 110.22, 90.00 |
Refinement procedure
| Resolution | 48.000 - 2.400 |
| R-factor | 0.219 |
| Rwork | 0.195 |
| R-free | 0.23630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5h0i |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.160 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.540 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.210 | 1.240 |
| Number of reflections | 41522 | 6542 |
| <I/σ(I)> | 5.78 | |
| Completeness [%] | 99.4 | |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 293 | PEG 3350, 0.2m Magnesium formate |
