9FHF

Crystal structure of human Glucose-6-phosphate isomerase with dihydroxyacetone phosphate ligand

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	2023-10-11
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.987
Spacegroup name	P 21 21 21
Unit cell lengths	80.676, 108.313, 271.497
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.050 - 1.800
R-factor	0.1878
Rwork	0.186
R-free	0.22760
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.092
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.050	1.864
High resolution limit [Å]	1.800	1.800
Rmerge	0.269	3.017
Rmeas	0.280	3.133
Rpim	0.076	0.836
Number of reflections	220113	21752
<I/σ(I)>	9.74	1.56
Completeness [%]	99.9	99.91
Redundancy	13.5	13.7
CC(1/2)	0.998	0.695

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	295	Protein buffer: 20 mM Tris pH 7.4, 30 mM NaCl, 20 dihydroxyacetone phosphate ligand. Reservoir: 21% w/v PEG3500, 0.16 M CaCl2, and 0.058 M HEPES, pH 7.0 Co-crystallization with ligand: Hanging drop: 1.5:0.5:1.5 ul - Protein (8 mg/ml):Seed stock:Reservoir. Cryoprotectant = a mixture containing the mother liquor, 24% v/v glycerol, and 15-20 mM ligand.