8P2R

Human Aldose Reductase Mutant A299G/L300A in Complex with a Ligand with an IDD Structure (3-({[2-(carboxymethoxy)-4-fluorobenzoyl]amino}methyl)benzoic 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)	0.918400
Spacegroup name	P 1 21 1
Unit cell lengths	47.335, 66.813, 49.298
Unit cell angles	90.00, 92.10, 90.00

Refinement procedure

Resolution	21.630 - 1.250
R-factor	0.1079
Rwork	0.107
R-free	0.13640
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.978
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]	49.270	1.330
High resolution limit [Å]	1.250	1.250
Number of reflections	76528	7826
<I/σ(I)>	21.63	3.97
Completeness [%]	90.2	57.2
Redundancy	6.5	4.9
CC(1/2)	0.999	0.912

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+, 12% (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