7F5J
The crystal structure of VyPAL2-I244V, a more efficient mutant of VyPAL2 peptide asparaginyl ligase in its active enzyme form
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 | 2020-10-20 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9537 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 76.270, 78.980, 92.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.060 - 1.593 |
Rwork | 0.163 |
R-free | 0.19270 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6idv |
RMSD bond length | 0.008 |
RMSD bond angle | 0.950 |
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] | 46.060 | 1.650 |
High resolution limit [Å] | 1.593 | 1.593 |
Rmerge | 0.083 | |
Rmeas | 0.086 | |
Rpim | 0.024 | 0.882 |
Number of reflections | 74533 | 6869 |
<I/σ(I)> | 16.5 | 0.83 |
Completeness [%] | 99.3 | 92.83 |
Redundancy | 13.4 | 12.5 |
CC(1/2) | 0.999 | 0.449 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.1 M Bis-Tris pH 5.5, 25% PEG 3350 |