6CIA

Crystal structure of aldo-keto reductase from Klebsiella pneumoniae in complex with NADPH.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2017-04-08
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 32 2 1
Unit cell lengths	83.626, 83.626, 72.834
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.300
R-factor	0.17052
Rwork	0.167
R-free	0.22957
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4wgh
RMSD bond length	0.010
RMSD bond angle	1.363
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0189)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.340
High resolution limit [Å]	2.300	2.300
Rmerge	0.083	1.092
Rmeas	0.088	1.178
Rpim	0.030	0.438
Number of reflections	13360	649
<I/σ(I)>	30.9	1.9
Completeness [%]	100.0	100
Redundancy	8.3	7
CC(1/2)	1.000	0.838

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	289.15	0.2 ul of 11 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 Top 96 #90 (0.2 uL 0.1 M Tris: HCl, pH 8.5, 25 % (w/v) PEG 3350) and 0.1 uL 30%v/v Ethanol (Additive Screen #82) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci)