Crystallization and preliminary X-ray analysis of L-methionine γ-lyase 1 from Entamoeba histolytica

L-Methionine gamma-lyase (MGL) is a pyridoxal phosphate-dependent enzyme that is involved in the degradation of sulfur-containing amino acids. MGL is an attractive drug target against amoebiasis because the mammalian host of its causative agent Entamoeba histolytica lacks MGL. For the development of antiamoebic agents based on the structure of MGL, one of two MGL isoenzymes (EhMGL1) was crystallized in the monoclinic space group P2(1), with unit-cell parameters a = 99.12, b = 85.38, c = 115.37 angstrom, beta = 101.82 degrees. The crystals diffract to beyond 2.0 angstrom resolution. The presence of a tetramer in the asymmetric unit (4 x 42.4 kDa) gives a Matthews coefficient of 2.8 angstrom(3) Da(-1) and a solvent content of 56%. The structure was solved by the molecular-replacement method and structure refinement is now in progress.