6Y03

Structure of Human Aldose Reductase Mutant L300/301A with a Citrate Molecule Bound in the Anion Binding Pocket

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-02-16
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.979003
Spacegroup name	P 1 21 1
Unit cell lengths	47.032, 66.373, 49.034
Unit cell angles	90.00, 92.26, 90.00

Refinement procedure

Resolution	49.000 - 1.690
R-factor	0.1623
Rwork	0.161
R-free	0.19530
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4prr
RMSD bond length	0.009
RMSD bond angle	1.018
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.16_3549)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.000	1.710
High resolution limit [Å]	1.620	1.620
Number of reflections	37291	5217
<I/σ(I)>	10.2	3.44
Completeness [%]	96.4	84
Redundancy	3.68	3.33
CC(1/2)	0.993	0.876

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	291	50 mM Di-Ammoniumhydrogen citrate pH 5: 15 mg/mL hAR, 5,2 mg/mL DTT, 0.7 mg/mL NADP+, 5% (w/v) PEG 6000 Reservoir: 120 mM Di-Ammoniumhydrogen citrate pH 5, 20% (w/v) PEG 6000