5UNL

Crystal structure of a D-beta-hydroxybutyrate dehydrogenase from Burkholderia multivorans

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2016-06-22
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	64.380, 132.090, 64.530
Unit cell angles	90.00, 108.68, 90.00

Refinement procedure

Resolution	50.000 - 1.650
R-factor	0.1757
Rwork	0.175
R-free	0.20770
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4nbv
RMSD bond length	0.006
RMSD bond angle	0.811
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	44.862	1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.064	0.034	0.497
Rmeas	0.074	0.039	0.570
Number of reflections	121380	1393	8916
<I/σ(I)>	13.99	30.85	2.83
Completeness [%]	99.1	98	98.8
Redundancy	4.17	3.837	4.202
CC(1/2)	0.998	0.998	0.827

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	JCSG+ A12 (272912a12): 20% w/v PEG3350, 200mM Potassium nitrate: protein conc 18mg/mL: 20% eg: icw9-5