9FCW

Crystal structure of human Glucose-6-phosphate isomerase with maleate 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)	0.976
Spacegroup name	P 21 21 21
Unit cell lengths	80.729, 107.295, 271.228
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.140 - 1.400
R-factor	0.1446
Rwork	0.142
R-free	0.18950
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.186
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]	38.140	1.450
High resolution limit [Å]	1.400	1.400
Rmerge	0.128	2.239
Rmeas	0.133	2.374
Rpim	0.037	0.756
Number of reflections	454749	41170
<I/σ(I)>	11.96	1.47
Completeness [%]	98.6	89.35
Redundancy	12.9
CC(1/2)	0.999	0.478

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 mM Malate 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.