6LKO
Turning an asparaginyl endopeptidase into a peptide ligase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-11-10 |
| Detector | DECTRIS PILATUS 2M-F |
| Wavelength(s) | 1.000030 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 44.550, 79.740, 135.020 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.310 - 2.000 |
| R-factor | 0.1938 |
| Rwork | 0.193 |
| R-free | 0.20520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6l4v |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.343 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.17_3644) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.310 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.093 | 1.076 |
| Number of reflections | 60392 | 3230 |
| <I/σ(I)> | 22.66 | |
| Completeness [%] | 100.0 | |
| Redundancy | 13 | |
| CC(1/2) | 1.000 | 0.784 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 20% v/v PEG 500* MME, 10 % w/v PEG 20000, 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 Sodium HEPES, MOPS (acid) |
