5THK

Crystal Structure of a Putative Dehydrogenase from Burkholderia cenocepacia with bound NADP

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	2016-07-05
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 1 21 1
Unit cell lengths	75.540, 102.440, 122.250
Unit cell angles	90.00, 97.28, 90.00

Refinement procedure

Resolution	45.192 - 1.400
R-factor	0.1399
Rwork	0.140
R-free	0.16410
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3u5t
RMSD bond length	0.005
RMSD bond angle	0.846
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((dev_2499))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]			1.440
High resolution limit [Å]	1.400	6.260	1.400
Rmerge	0.062	0.024	0.560
Number of reflections	358521
<I/σ(I)>	14.28	42.08	2.38
Completeness [%]	99.1	97.9	98.7
Redundancy	3.8
CC(1/2)	0.999	0.999	0.769

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	BuceA.00010.k.B1.PW37237 @22.1 mg/ml, incubated with 4mM NADP, mixed 1:1 with an equal volume MCSG1(e3): 30% (v/v) PEG 550 MME, 0.1 M HEPES/NaOH, pH=7.5, 0.05 M MgCl2