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

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 P2(1)2(1)2(1), 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.

SUBMITTER: Yeo SJ

PROVIDER: S-EPMC3433200 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

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

Yeo Seung-Joo SJ Jeong Jae-Hee JH Yu Sun-Nam SN Kim Yeon-Gil YG

Acta crystallographica. Section F, Structural biology and crystallization communications 20120830 Pt 9

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. ...[more]

PMID: 22949197

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