4XK2

Crystal structure of aldo-keto reductase from Polaromonas sp. JS666

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2014-07-23
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.979
Spacegroup name	I 4 2 2
Unit cell lengths	105.110, 105.110, 479.569
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.900
R-factor	0.1617
Rwork	0.161
R-free	0.18470
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jtd
RMSD bond length	0.009
RMSD bond angle	1.261
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0049)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.930
High resolution limit [Å]	1.900	5.160	1.900
Rmerge	0.082	0.034	0.830
Rmeas	0.090	0.037	0.910
Rpim	0.036	0.015	0.373
Total number of observations	630404
Number of reflections	106320
<I/σ(I)>	5.8		1.9
Completeness [%]	100.0	99.5	100
Redundancy	5.9	5.7	5.8
CC(1/2)		0.998	0.702

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	0.2 ul of 12 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of the MCSG Suite 3 condition #81 (0.2M NaCl, 0.1M Na citrate, 40%v/v 1,2-propanodiol pH=5.5) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). Before crystallization protein was incubated with 1/50 v/v of 2 mg/ml chymotrypsin solution at 289 K for 3 hours.