1EF3

FIDARESTAT BOUND TO HUMAN ALDOSE REDUCTASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	MACSCIENCE
Temperature [K]	281
Detector technology	IMAGE PLATE
Collection date	1998-07-06
Detector	MAC Science DIP-2000
Spacegroup name	C 1 2 1
Unit cell lengths	96.140, 62.560, 118.990
Unit cell angles	90.00, 101.60, 90.00

Refinement procedure

Resolution	8.000 - 2.800
R-factor	0.191
Rwork	0.186
R-free	0.27800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ads
RMSD bond length	0.014
RMSD bond angle	23.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	999.000	2.850
High resolution limit [Å]	2.800	2.800
Rmerge	0.070
Total number of observations	27091 *
Number of reflections	15960
Completeness [%]	92.4	81.7
Redundancy	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	277	1.8M ammonium sulfate, 2% PEG400, 0.1 M HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	1.8 (M)
2	1	reservoir	PEG400	2 (%)
3	1	reservoir	HEPES/NaOH	0.1 (M)