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  • Title: Purification and preliminary X-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli.
    Author: Käck H, Gibson KJ, Gatenby AA, Schneider G, Lindqvist Y.
    Journal: Acta Crystallogr D Biol Crystallogr; 1998 Nov 01; 54(Pt 6 Pt 2):1397-8. PubMed ID: 10089517.
    Abstract:
    Recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli, a pyridoxal-phosphate-dependent aminotransferase, has been crystallized in space groups P21 and C2. Both crystal forms were obtained at pH 7.3 with 21% polyethylene glycol and 10% 2-propanol as precipitants. The cell dimensions were a = 130, b = 57.5, c = 117 A, beta = 110 degrees for the C2 crystals, and a = 58.4, b = 55.6, c = 121 A, beta = 96.9 degrees for the P21 crystals, which diffract to at least 2.6 and 2.0 A resolution, respectively.
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