8Q8H

Crystal Structure of Apo beta-D-GalNAcase from Niabella aurantiaca (Structure 2)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX IV BEAMLINE BioMAX
Synchrotron site	MAX IV
Beamline	BioMAX
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-12-07
Detector	DECTRIS EIGER2 S 16M
Wavelength(s)	0.976254
Spacegroup name	P 21 21 2
Unit cell lengths	173.640, 195.570, 82.040
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.290 - 2.500
R-factor	0.1902
Rwork	0.188
R-free	0.23200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	1.402
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.810	2.650
High resolution limit [Å]	2.500	2.500
Number of reflections	97317	15552
<I/σ(I)>	13.14
Completeness [%]	100.0	100
Redundancy	6.85
CC(1/2)	0.990	0.530

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.4	277	Protein at 8 mg/ml was crystallised by mixing 200 nl protein with 100 nl of 0.2 M ammonium sulfate, 20 % w/v PEG 3350. Drops were supplemented with 20% glycerol for cryo-protection