5VML

Crystal Structure of Acetoacetyl-CoA Reductase from Burkholderia Pseudomallei 1710b with bound NADP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2017-03-02
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 42 21 2
Unit cell lengths	66.310, 66.310, 115.260
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.888 - 1.700
R-factor	0.1461
Rwork	0.144
R-free	0.17090
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ezl
RMSD bond length	0.005
RMSD bond angle	0.772
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX ((dev_2744))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.740
High resolution limit [Å]	1.700	1.700
Rmerge	0.062	0.458
Number of reflections	28909	1965
<I/σ(I)>	22.03
Completeness [%]	99.5	93.2
Redundancy	8.9	4.3
CC(1/2)	0.999	0.856

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	BupsA.00010.e.A1.PS00061 at 19.3 mg/ml incubated with 4 mM NADP, mixed 1:1 with Morpheus(c8): 12.5% (w/v) PEG-1000, 12.5% (w/v) PEG-3350, 12.5% (v/v) MPD, 0.1 M MOPS/ HEPES-Na, pH = 7.5, 0.03 M each sodium nitrate, disodium hydrogen phosphate, ammonium sulfate, crystals were soaked for 24 hours with 5 mM NADP in well solution, harvested directly