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

Autor:	Johansson, Eva, Steffens, James J., Emptage, Mark, Lindqvist, Ylva, Schneider, Gunter
Předmět:	PYRICULARIA grisea CLONING AMMONIUM sulfate HYDROGEN-ion concentration GENETIC engineering PATHOGENIC microorganisms
Zdroj:	Acta Crystallographica: Section D (Wiley-Blackwell); May2000, Vol. 56 Issue 5, p662-664, 3p
Abstrakt:	The gene coding for saccharopine reductase (E.C. 1.5.1.10), an enzyme of the α-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 C2221 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 Å, β = 111.1° for space group C2, and a = 89.3, b = 119.0, c = 195.9 Å for space group C2221. The crystals diffract to resolutions of 2.0 Å (C2) and 2.4 Å (C2221) at synchrotron sources. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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