PMID:10089517

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Citation

Käck, H, Gibson, KJ, Gatenby, AA, Schneider, G and Lindqvist, Y (1998) Purification and preliminary X-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 54:1397-8

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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Keywords

Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Protein Conformation; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/isolation & purification; Transaminases/chemistry; Transaminases/isolation & purification

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