5VT6

Crystal structure of Acetoacetyl-CoA Reductase from Burkholderia pseudomallei 1710b complexed with NADP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.1
Synchrotron site	ALS
Beamline	8.2.1
Temperature [K]	100
Detector technology	CCD
Collection date	2017-05-03
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.0000
Spacegroup name	P 1 21 1
Unit cell lengths	73.150, 92.180, 83.050
Unit cell angles	90.00, 115.15, 90.00

Refinement procedure

Resolution	39.293 - 1.700
R-factor	0.1442
Rwork	0.144
R-free	0.17260
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ftp
RMSD bond length	0.006
RMSD bond angle	0.823
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	39.293	39.293	1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge	0.064	0.019	0.544
Rmeas	0.075	0.022	0.649
Total number of observations	409125
Number of reflections	109414	1270	8064
<I/σ(I)>	16.25	46.73	2.31
Completeness [%]	99.7	97.8	99.7
Redundancy	3.739	3.686	3.38
CC(1/2)	0.998	0.999	0.748

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	290	8.175 mg/mL BupsA.00010.g.A1.PS00076 in 8 mM NADP, mixed 1:1 with TOP96(h9) (10% w/v PEG8000, 0.1 M imidazole/HCl, pH = 8.0, 0.2 M calcium acetate), harvested with 20% ethylene glycol