Crystallization and preliminary X‐ray crystallographic analysis of YgjG from Escherichia coli

E-ISSN： 1744-3091|68|9|1070-1072

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.68, Iss.9, 2012-09, pp. : 1070-1072

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Abstract

Putrescine, one of the polyamines that are found in virtually all living organisms, has been implicated as an important biological material. The protein YgjG is involved in the putrescine‐degradation pathway in Escherichia coli. The enzyme is a putrescine:2‐oxoglutarate aminotransferase that belongs to the class III aminotransferases. In this study, YgjG from E. coli was overexpressed, purified and crystallized using the hanging‐drop vapour‐diffusion method. Diffraction data were collected to 2.1 Å resolution using synchrotron radiation. The crystal belonged to the primitive orthorhombic space group P2₁2₁2₁, with unit‐cell parameters a = 121.1, b = 129.5, c = 131.3 Å, and is estimated to contain four molecules of YgjG per asymmetric unit.