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• W2066862624 abstract "l-Methionine γ-lyase (MGL) is considered to be an attractive target for rational drug development because the enzyme is absent in mammalian hosts. To enable structure-based design of drugs targeting MGL, one of the two MGL isoenzymes (EhMGL2) was crystallized in the orthorhombic space group P212121, with unit-cell parameters a = 88.89, b = 102.68, c = 169.87 Å. The crystal diffracted to a resolution of 2.0 Å. The presence of a tetramer in the asymmetric unit (4 × 43.1 kDa) gives a Matthews coefficient of 2.2 Å3 Da−1. The structure was solved by the molecular-replacement method and structure refinement is now in progress." @default.
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• W2066862624 date "2006-09-30" @default.
• W2066862624 modified "2023-10-16" @default.
• W2066862624 title "Expression, purification and crystallization of<scp>L</scp>-methionine γ-lyase 2 from<i>Entamoeba histolytica</i>" @default.
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• W2066862624 doi "https://doi.org/10.1107/s1744309106036694" @default.
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