9SN8

Crystal structure of anthocyanin-related glutathione transferase from bilberry

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-3
Synchrotron site	ESRF
Beamline	MASSIF-3
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-11-11
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.967697
Spacegroup name	P 1 21 1
Unit cell lengths	56.294, 159.117, 90.374
Unit cell angles	90.00, 95.60, 90.00

Refinement procedure

Resolution	89.940 - 2.340
Rwork	0.210
R-free	0.24260
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.854
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0430 (refmacat 0.4.100))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	89.940	2.400
High resolution limit [Å]	2.340	2.340
Rmerge	0.105	0.637
Number of reflections	65742	4594
<I/σ(I)>	4.8	1.1
Completeness [%]	98.8	99
Redundancy	3.5	3.7
CC(1/2)	0.992	0.612

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION		277	Precipitating solution : - 20% v/v Ethylene glycol / 10 % w/v PEG 8000 - 0,1 M Buffer System 1 pH 6,5 (Buffer System 1 : 1.0M, pH6.5 -> Imidazole; MES monohydrate (acid)) - 0,1 M Amino acids (0.2M DL-Glutamic acid monohydrate; 0.2M DL-Alanine; 0.2M Glycine; 0.2M DL-Lysine monohydrochloride; 0.2M DL-Serine) Protein solution : 14.9 mg/mL protein in 20 mM Tris-HCl pH 8.0 ; 200 mM NaCl ; 1mM EDTA