5IZ4

Crystal structure of a putative short-chain dehydrogenase/reductase from Burkholderia xenovorans

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	2016-03-17
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	I 4 2 2
Unit cell lengths	84.610, 84.610, 135.250
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.865 - 1.750
R-factor	0.1543
Rwork	0.152
R-free	0.18200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4e3z
RMSD bond length	0.005
RMSD bond angle	0.797
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	PHENIX (dev_2356)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	35.865	35.865	1.800
High resolution limit [Å]	1.750	7.830	1.750
Rmerge	0.058	0.029	0.529
Number of reflections	25142
<I/σ(I)>	30.22	72.91	4.64
Completeness [%]	99.9	96.5	99.9
Redundancy	12
CC(1/2)	1.000

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	Microlytic Morpheus f12: 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD; 20mM of each D-glucose, D-mannose, D-galactose, L-fucose, D-xylose, N-acetyld-glucosamine; 10mM bicine/Trizma base pH 8.5; BuxeA.00010.e.B1.PS37833 at 12.8mg/ml + 3mM NAD, direct cryo; tray: 270602f12, puck jra0-6; only the ADP moiety of NAD was observed in the density