6BN2

Crystal structure of Acetyl-CoA acetyltransferase from Elizabethkingia anophelis NUHP1

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	2016-10-12
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	C 2 2 2
Unit cell lengths	99.170, 167.420, 72.560
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.939 - 1.650
R-factor	0.1389
Rwork	0.138
R-free	0.15610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3LSQ per MorDa
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]	40.939	40.939	1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.053	0.023	0.511
Rmeas	0.057	0.025	0.570
Number of reflections	72724	901	5325
<I/σ(I)>	20.87	50.18	3.06
Completeness [%]	99.9	97.9	100
Redundancy	6.028	5.452	5.099
CC(1/2)	0.999	0.999	0.860

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	285	18.9 mg/mL ElanA.00654.a.B1.PS38241 + 3 mM AcetylCoA + RigakuReagents JCSG+ screen, E11: 14.5% w/v PEG8000, 20% w/v glycerol, 160 mM calcium acetate, 100 mM cacodylate/HCl, pH 6.5, cryoprotectant: direct, tray 291032e11, puck DYA4-6