Open AccessCrystallization and preliminary X‐ray crystallographic analysis of YgjG from Escherichia coli
Author(s) -
Yeo SeungJoo,
Jeong JaeHee,
Yu SunNam,
Kim YeonGil
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112030886
Subject(s) - orthorhombic crystal system , putrescine , escherichia coli , crystallization , crystallography , x ray , chemistry , synchrotron radiation , x ray crystallography , molecule , resolution (logic) , enzyme , diffraction , crystal structure , biochemistry , organic chemistry , physics , optics , artificial intelligence , computer science , gene
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 P 2 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.