title: 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.
authors.affiliation: Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, Republic of Korea.
authors.forename: Seung-Joo
authors.initials: SJ
authors.lastname: Yeo
authors.forename: Jae-Hee
authors.initials: JH
authors.lastname: Jeong
authors.forename: Sun-Nam
authors.initials: SN
authors.lastname: Yu
authors.forename: Yeon-Gil
authors.initials: YG
authors.lastname: Kim
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D000637:Transaminases / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D000637:Transaminases; C507750:YgjG protein, E coli