Truncated Human ATP-Citrate Lyase with Citrate Bound

Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography.

Truncated Human ATP-Citrate Lyase (UNP residues 1-425)

Truncated Human ATP-Citrate Lyase (UNP residues 487-820)

ATP-citrate (pro-S-)-lyase, Citrate cleavage enzyme

10% (w/v) PEG 3350, 75 mM potassium citrate, 100 mM Tris-HCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K

Truncated Human ATP-Citrate Lyase with Tartrate Bound

CRYSTALS WERE GROWN WITH LIMITED PROTEOLYIS BY STARTING WILL FULL LENGTH PROTEIN AND EXPRESSION TAG. BY SDS-PAGE ANALYSIS OF DISSOLVED CRYSTALS AND SUBSEQUENT MASS SPECTROMETRY TWO CRYSTALLIZED PORTIONS WERE IDENTIFIED.

ATP-grasp, phosphohistidine, organic acid, LYASE, TRANSFERASE