9FKC

Crystal structure of human Glucose-6-phosphate isomerase with citraconate 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	2023-12-12
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.987
Spacegroup name	P 21 21 21
Unit cell lengths	80.723, 107.838, 271.481
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.320 - 1.600
R-factor	0.1993
Rwork	0.198
R-free	0.22720
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.771
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]	46.320	1.657
High resolution limit [Å]	1.600	1.600
Rmerge	0.177	3.608
Rmeas	0.187	3.816
Rpim	0.061	1.232
Number of reflections	310523	30661
<I/σ(I)>	8.66	0.93
Completeness [%]	99.7	99.1
Redundancy	9.1	9.2
CC(1/2)	0.998	0.464

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 citraconate 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.