Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea

The gene coding for saccharopine reductase (E.C. 1.5.1.10), an enzyme of th e alpha-aminoadipic pathway of lysine biosynthesis in the pathogenic fungus Magnaporthe grisea, was cloned and expressed in Escherichia coli. The puri fied enzyme was crystallized in space groups C2 and C222(1) using ammonium sulfate pH 4.8 or PEG 6000 pH 4.1 as precipitants. The unit-cell parameters are a = 115.0, b = 56.6, c = 74.3 Angstrom, beta = 111.1 degrees for space group C2, and a = 89.3, b = 119.0, c = 195.9 Angstrom for space group C222 (1). The crystals diffract to resolutions of 2.0 Angstrom (C2) and 2.4 Angs trom (C222(1)) at synchrotron sources.