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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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 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.[1]

References

  1. Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea. Johansson, E., Steffens, J.J., Emptage, M., Lindqvist, Y., Schneider, G. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
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