Crystallization and preliminary X‐ray analysis of l‐methionine γ‐lyase 1 from Entamoeba histolytica

l-Methionine γ-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 anti-amoebic agents based on the structure of MGL, one of two MGL isoenzymes (EhMGL1) was crystallized in the monoclinic space group P21, with unit-cell parameters a = 99.12, b = 85.38, c = 115.37 A, β = 101.82°. The crystals diffract to beyond 2.0 A resolution. The presence of a tetramer in the asymmetric unit (4 × 42.4 kDa) gives a Matthews coefficient of 2.8 A3 Da−1 and a solvent content of 56%. The structure was solved by the molecular-replacement method and structure refinement is now in progress.