Display Settings:

Format

Send to:

Choose Destination

    Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):662-4.

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

    Johansson E, Steffens JJ, Emptage M, Lindqvist Y, Schneider G.

    Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden.

    The gene coding for saccharopine reductase (E.C. 1.5.1.10), an enzyme of the alpha-aminoadipic pathway of lysine biosynthesis in the pathogenic fungus Magnaporthe grisea, was cloned and expressed in Escherichia coli. The purified 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 A, beta = 111.1 degrees for space group C2, and a = 89.3, b = 119.0, c = 195.9 A for space group C222(1). The crystals diffract to resolutions of 2.0 A (C2) and 2.4 A (C222(1)) at synchrotron sources.

    PMID: 10771443 [PubMed - indexed for MEDLINE]

    Supplemental Content

    Click here to read

    Structures reported by this article