8OZ2

Human Aldose Reductase Mutant A299G/L300A in Complex with a Ligand with an IDD Structure ({5-fluoro-2-[(3-nitrobenzyl)carbamoyl]phenoxy}acetic acid)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-06-28
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.9184
Spacegroup name	P 1 21 1
Unit cell lengths	47.405, 66.349, 49.300
Unit cell angles	90.00, 92.38, 90.00

Refinement procedure

Resolution	21.080 - 1.040
R-factor	0.1106
Rwork	0.110
R-free	0.12380
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.010
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.360	1.100
High resolution limit [Å]	1.040	1.040
Number of reflections	138578	16995
<I/σ(I)>	17.74	2.46
Completeness [%]	94.5	71.7
Redundancy	6.3	4.1
CC(1/2)	0.990	0.800

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	291	50 mM Di-Ammoniumhydrogen citrate pH 5: 15 mg/mL hAR, 5.2 mg/mL DTT, 0.7 mg/mL NADP+, 11.5% (w/v) PEG 6000; Reservoir: 120 mM Di-Ammoniumhydrogen citrate pH 5, 20% (w/v) PEG 6000; Soaking: 120 mM di-ammonium hydrogen citrate pH 5.0, 25% PEG 6000, saturated ligand