7F5Q
The crystal structure of VyPAL2 peptide asparaginyl ligase in its active enzyme form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL32XU |
Synchrotron site | SPring-8 |
Beamline | BL32XU |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-10-16 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.99999 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 63.570, 63.880, 151.880 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.880 - 2.300 |
Rwork | 0.175 |
R-free | 0.21740 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6idv |
RMSD bond length | 0.007 |
RMSD bond angle | 1.429 |
Data reduction software | autoPROC |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.880 | 2.382 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.419 | 2.141 |
Number of reflections | 28255 | 2779 |
<I/σ(I)> | 7.51 | 1.32 |
Completeness [%] | 100.0 | 100 |
Redundancy | 10.3 | 10.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4 | 293.15 | 0.2 M lithium sulfate, 0.1 M sodium acetate, pH 4.5, 30% PEG 8000 |