9F69

Crystal structure of human triose phosphate isomerase with methyl malonic acid 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	48.466, 48.466, 341.862
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	31.830 - 1.170
R-factor	0.1484
Rwork	0.146
R-free	0.18370
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.047
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]	31.830	1.212
High resolution limit [Å]	1.170	1.170
Rmerge	0.116
Rpim	0.020	0.661
Number of reflections	82312	8037
<I/σ(I)>	23.55	1.23
Completeness [%]	99.8	99.06
Redundancy	34.8	20.4
CC(1/2)	0.999	0.437

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		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 24 mM methylmalonate (pH adjusted to 7.4), mother liquor, and cryo-protectant Ligand soaking and cryoprotectant were performed simultaneously