9FKF

Crystal structure of human Glucose-6-phosphate isomerase with phosphoenol pyruvate 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	80.840, 107.482, 271.193
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.420 - 1.600
R-factor	0.1887
Rwork	0.187
R-free	0.22350
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.015
RMSD bond angle	1.358
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]	48.420	1.657
High resolution limit [Å]	1.600	1.600
Rmerge	0.193	3.025
Rmeas	0.201	3.142
Rpim	0.054	0.844
Number of reflections	310109	30723
<I/σ(I)>	9.89	1.49
Completeness [%]	99.8	99.79
Redundancy	13.5	13.6
CC(1/2)	0.999	0.671

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 PEP 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.