9LFR

Crystal of Glucosidase form Ophiorrhiza pumila

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL19U1
Synchrotron site	SSRF
Beamline	BL19U1
Temperature [K]	277.15
Detector technology	PIXEL
Collection date	2024-06-21
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97861
Spacegroup name	I 4 2 2
Unit cell lengths	136.990, 136.990, 164.750
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	82.380 - 1.780
R-factor	0.1939
Rwork	0.193
R-free	0.21850
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.896
Data reduction software	autoPX
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	82.380	1.844
High resolution limit [Å]	1.780	1.780
Number of reflections	74660	7391
<I/σ(I)>	22.92
Completeness [%]	99.8
Redundancy	1.999
CC(1/2)	1.000	0.617

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	4.6	291.15	Purified OpBGlu1 proteins at a concentration of 6 mg/mL was combined with an equal volume of reservoir solution containing 0.1 M sodium acetate at pH of 4.6 and 2.0 ammonium sulfate. Consistent with the conditions under which loganetin was added, the reservoir solution consisted of 0.1 M sodium acetate trihydrate at pH 4.5 and 2.0 M ammonium sulfate. The sessile drop plate was covered with an adhesive tape and incubated in a cabinet maintained at a temperature of 291.15 K. Diffraction-quality crystals were produced within a time-frame of 10 to 15 days.