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- W1998492007 abstract "Aspartate-β-semialdehyde dehydrogenase catalyzes the NADPH-mediated reductive dephosphorylation of β-aspartylphosphate at a branch point in the biosynthesis of several amino acids. The enzyme from Escherichia coli has been crystallized by the vapor diffusion method from Tris buffer (pH 8.5) using polyethylene glycol 4000 as a precipitant. The crystals are orthorhombic and have the symmetry of space group P2221, with unit cell dimensions of a = 177.8 Å, b = 59.9 Å, c = 118.65 Å, and α = β = γ = 90 °. The dimensions and space group are indicative of two enzyme dimers (40 kDa per subunit) in the asymmetric unit. The crystals show strong diffraction, and a native data set has been collected to 2.5 Å resolution." @default.
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- W1998492007 date "1992-11-01" @default.
- W1998492007 modified "2023-09-24" @default.
- W1998492007 title "Crystallization and preliminary crystallographic analysis of aspartate-β-semialdehyde dehydrogenase from Escherichia coli" @default.
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- W1998492007 doi "https://doi.org/10.1016/0022-2836(92)90508-h" @default.
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