9CSJ

Crystal structure of human glyoxalase domain-containing protein 4 (GLOD4) at 2.33 A resolution.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, DESY BEAMLINE P11
Synchrotron site	PETRA III, DESY
Beamline	P11
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-03-06
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.97918
Spacegroup name	P 41
Unit cell lengths	85.960, 85.960, 135.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.340 - 2.330
R-factor	0.22267
Rwork	0.220
R-free	0.26902
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.502
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.340	2.410
High resolution limit [Å]	2.330	2.330
Rmerge	0.163	1.253
Rmeas	0.169
Rpim	0.045	0.354
Number of reflections	42055	4088
<I/σ(I)>	13.2
Completeness [%]	99.9
Redundancy	14.1	13.3
CC(1/2)	0.998	0.842

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	7.3	291	GLOD4 aa2-298 with an N-terminal 8-His tag was expressed in E. coli, purified by IMAC and SEC, and stored in 50 mM HEPES (pH 7.5), 500 mM NaCl, and 5% glycerol at -80 C. His-GLOD4 (18 mg/ml) was crystallized after Hist-tag removal in 34% PEG 3350, 200 mM MgCl2, and 50 mM HEPES, pH 7.3.