7F5P
The crystal structure of VyPAL2-C214A, a dead mutant of VyPAL2 peptide asparaginyl ligase in form I
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 | 2021-04-30 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.95373 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 95.000, 81.150, 47.650 |
| Unit cell angles | 90.00, 113.62, 90.00 |
Refinement procedure
| Resolution | 40.910 - 1.900 |
| Rwork | 0.215 |
| R-free | 0.24440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6idv |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.020 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.910 | 1.968 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 26508 | 2523 |
| <I/σ(I)> | 8.85 | 0.68 |
| Completeness [%] | 99.3 | 97.63 |
| Redundancy | 26.5 | 19.2 |
| CC(1/2) | 0.998 | 0.543 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.2 M lithium sulfate, 0.1 M sodium acetate, pH 4.6, 30% PEG 8000 |
