7FA0
The crystal structure of VyPAL2-C214A, a dead mutant of VyPAL2 peptide asparaginyl ligase in form II
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-06-03 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.00001 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.495, 78.546, 92.670 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.330 - 1.800 |
| R-factor | 0.1688 |
| Rwork | 0.164 |
| R-free | 0.19440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6idv |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.960 |
| Data reduction software | autoPROC |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.330 | 1.864 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.091 | 1.008 |
| Rmeas | 0.099 | 1.100 |
| Rpim | 0.038 | 0.434 |
| Number of reflections | 51971 | 5111 |
| <I/σ(I)> | 12.65 | 2.12 |
| Completeness [%] | 99.1 | 98.35 |
| Redundancy | 6.7 | 6.2 |
| CC(1/2) | 0.997 | 0.698 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.2 M Potassium formate, 20% PEG 3350 |
