8PUO

Structural determinants of cold-activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas Ef 1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-3
Synchrotron site	ESRF
Beamline	MASSIF-3
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-10-31
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.9677
Spacegroup name	P 21 21 2
Unit cell lengths	103.116, 201.120, 47.825
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.880 - 1.800
R-factor	0.1653
Rwork	0.165
R-free	0.18930
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.018
RMSD bond angle	1.270
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	PHENIX ((1.20.1_4487))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	67.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.083	0.986
Rmeas	0.087	1.038
Number of reflections	91533	12892
<I/σ(I)>	16.2	2.3
Completeness [%]	98.3	96
Redundancy	10.7	9.2
CC(1/2)	0.999	0.805

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	M-GH1 crystals grew over 2-4 days in 50% protein drop in an optimized condition of PACT condition G1, containing 22% (w/v) PEG 3500, 0.1 M sodium fluoride (NaF) and 0.1 M Tris-HCl pH 8.5.