2.3.3.8	full structure of human ACLY homotetramer in ternary complex with the inhibitor and ADP with an overall resolution of 3.67 A	
2.3.3.8	in complex with citrate or tartrate, hanging drop vapor diffusion method, using either 12.5% (w/v) PEG 3350, 100 mM sodium tartrate, 100 mM Tris-HCl (pH 7.0) for the native protein or 10% PEG 3350, 75 mM potassium citrate, 100 mM Tris-HCl (pH 7.0) for the selenomethionyl protein	
2.3.3.8	in the presence of tartrate, ATP and magnesium ions	
2.3.3.8	tartrate and ADP-Mg2+ bound N-terminal portion of the enzyme containing residues 1-817, hanging drop vapor diffusion method, using 12.5% (w/v) polyethylene glycol 3350, 125 mM sodium tartrate, 100 mM Tris-HCl (pH 8.2)	
2.3.3.8	vapour diffusion crystallization	
2.3.3.8	vapour diffusion in hanging drops. The protein is modified by introducing cleavage sites for Tobacco etch virus protease on either side of a disordered linker. The protein crystallized consists of residues 2-425-ENLYFQ and S-488-810 of human ATP-citrate lyase. When co-crystals are grown with ATP and magnesium ions as well as either the inhibitor (2S,3S)-2-hydroxycitrate or citrate, Mg2+-ADP is bound and His760 is phosphorylated