5H0I
Structure of OaAEP1 asparaginyl peptide ligase in its proenzyme form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 77 |
| Detector technology | PIXEL |
| Collection date | 2016-06-17 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 145.730, 70.210, 118.280 |
| Unit cell angles | 90.00, 117.14, 90.00 |
Refinement procedure
| Resolution | 71.720 - 2.560 |
| R-factor | 0.187 |
| Rwork | 0.186 |
| R-free | 0.22400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nok |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.190 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 71.720 | 2.700 |
| High resolution limit [Å] | 2.560 | 2.560 |
| Rmerge | 0.095 | 0.700 |
| Number of reflections | 34420 | |
| <I/σ(I)> | 7 | 1.7 |
| Completeness [%] | 99.7 | 99.6 |
| Redundancy | 3 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 290 | 200mM NH4NO3, pH ~ 4.5, 13-15%(w/v) PEG 3,350 with 10%(v/v) glycerol or ethylene glycol |
