Purification and preliminary X-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli

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 Å, β = 110° for the C2 crystals, and a = 58.4, b = 55.6, c = 121 Å, β = 96.9° for the P2₁ crystals, which diffract to at least 2.6 and 2.0 Å resolution, respectively.