6L4Y
Turning an asparaginyl endopeptidase into a peptide ligase
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 | 2018-03-05 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.953736 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.610, 79.600, 136.470 |
| Unit cell angles | 90.00, 93.95, 90.00 |
Refinement procedure
| Resolution | 21.840 - 1.500 |
| R-factor | 0.1724 |
| Rwork | 0.172 |
| R-free | 0.19030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6l4v |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.960 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 21.840 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.057 | 1.055 |
| Number of reflections | 151957 | 15107 |
| <I/σ(I)> | 11.01 | |
| Completeness [%] | 99.9 | |
| Redundancy | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7.2 | 298 | 0.1M Sodium formate, 0.1M Ammonium acetate, 0.1M Sodium citrate tribasic dihydrate, 0.1M Potassium sodium tartrate tetrahydrate, 0.1M Sodium oxamate, 0.1M HEPES, 0.1M MOPS, 10% Ethylen Glycol, 8% PEG8000 |
