3GK3

Crystal structure of acetoacetyl-CoA reductase from Burkholderia pseudomallei 1710b

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2008-10-06
Detector	RIGAKU SATURN 944
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	70.570, 102.920, 137.240
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.803 - 2.100
R-factor	0.228
Rwork	0.226
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.156
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	41.803		2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.089	0.022	0.558
Number of reflections	58501	713	4253
<I/σ(I)>		42.7	2.4
Completeness [%]	98.9	91.6	98

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	6.5	290	JCSG+ screen D12: 40mM KH2PO4, 16% PEG 8000, 20% glycerol, 0.4ul + 0.4ul, protein at 32.7mg/ml, pH 6.5, vapor diffusion, temperature 290K