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