9XG1

Crystal structure of protein-asparaginase from Amycolatopsis deserti

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE AR-NW12A
Synchrotron site	Photon Factory
Beamline	AR-NW12A
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-06-09
Detector	DECTRIS PILATUS3 S 2M
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	53.654, 99.750, 114.283
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.620 - 2.080
R-factor	0.18304
Rwork	0.180
R-free	0.24415
Structure solution method	MOLECULAR REPLACEMENT
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0405)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.570	2.140
High resolution limit [Å]	2.080	2.080
Rmerge	0.175
Number of reflections	37678	2896
<I/σ(I)>	9.2
Completeness [%]	100.0
Redundancy	6.6
CC(1/2)		0.715

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION		293	25% w/v polyethylene glycol 3,350 and Bis-Tris pH6.4