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