9FFC

Crystal structure of human triose phosphate isomerase with glycerol-3-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	2024-02-20
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.976
Spacegroup name	P 61 2 2
Unit cell lengths	48.860, 48.860, 342.156
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	25.060 - 1.250
R-factor	0.1478
Rwork	0.146
R-free	0.18010
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.049
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	MoRDa
Refinement software	REFMAC (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.060	1.295
High resolution limit [Å]	1.250	1.250
Rmerge	0.069	0.952
Rmeas	0.070	0.965
Rpim	0.012	0.157
Number of reflections	68952	6688
<I/σ(I)>	28.46	4.1
Completeness [%]	99.6	99.46
Redundancy	36.4
CC(1/2)	1.000	0.990

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	295	Protein buffer: 20 mM Tris pH 7.4, 30 mM NaCl. Reservoir: 0.14 M KBr, 24% PEG 2000 MME. Hanging drop: 1.5:1.5:1.0 ul - Reservoir-Protein (8 mg/ml)-Seed stock. Cryoprotectant = 20% glycerol; Ligand soaking performed for 5-6 min in a mixture containing 20 mM glycerol-3-phosphate (pH adjusted to 7.4), mother liquor, and cryo-protectant Ligand soaking and cryoprotectant were performed simultaneously