6T5G

Structure of Human Aldose Reductase Mutant L300A 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 PILATUS3 6M
Wavelength(s)	0.979003
Spacegroup name	P 1
Unit cell lengths	39.685, 46.717, 48.507
Unit cell angles	93.01, 116.86, 102.61

Refinement procedure

Resolution	44.900 - 1.280
R-factor	0.1311
Rwork	0.130
R-free	0.15950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4prr
RMSD bond length	0.012
RMSD bond angle	1.238
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]	44.900	1.350
High resolution limit [Å]	1.277	1.280
Number of reflections	69706	10022
<I/σ(I)>	6.11	2.42
Completeness [%]	89.6	79.9
Redundancy	2	2
CC(1/2)	0.986	0.793

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	291	50 mM Di-Ammoniumhydrogen citrate pH 5.0: 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 5.0, 20% (w/v) PEG 6006