3N2T

Structure of the glycerol dehydrogenase AKR11B4 from Gluconobacter oxydans

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Wavelength(s)	0.9537
Spacegroup name	P 1 21 1
Unit cell lengths	41.250, 62.390, 59.820
Unit cell angles	90.00, 90.47, 90.00

Refinement procedure

Resolution	24.119 - 2.000
R-factor	0.1907
Rwork	0.189
R-free	0.23160
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.963
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((phenix.refine: 1.5_2))

Data quality characteristics

	Overall
Low resolution limit [Å]	34.500
High resolution limit [Å]	2.000
Rmerge	0.133
Number of reflections	26999
<I/σ(I)>	10.1
Completeness [%]	99.8
Redundancy	5.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	protein stock solution: 10 mg/ml AKR11B4 protein, 10 mM Tris/HCl puffer, 150 mM NaCl, 0.5 mM EDTA, pH 8.5. Reservoir solution: 35 % (w/v) poly ethylen glycol 3350 (PEG 3350), 200 mM potassium nitrate. The crystallization drop contained equal volumes of the reservoir and the protein stock solution before equilibration. The pH-value in the crystallization drop was determined by the buffer of the protein stock solution., VAPOR DIFFUSION, SITTING DROP, temperature 293K