title: Purification, crystallization and preliminary crystallographic analysis of Est-Y29: a novel oligomeric beta-lactamase.
abstract: beta-Lactam antibiotics such as penicillins and cephalosporins have a four-atom ring as a common element in their structure. The beta-lactamases, which catalyze the inactivation of these antibiotics, are of great interest because of their high incidence in pathogenic bacteria. A novel oligomeric class C beta-lactamase (Est-Y29) from a metagenomic library was expressed, purified and crystallized. The recombinant protein was expressed in Escherichia coli with an N-terminal 6xHis tag and purified to homogeneity. EstY-29 was crystallized and X-ray intensity data were collected to 1.49 A resolution using synchrotron radiation.
authors.affiliation: Department of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
authors.forename: Seungbum
authors.initials: S
authors.lastname: Kim
authors.forename: Sangbum
authors.initials: S
authors.lastname: Joo
authors.forename: Sangyoung
authors.initials: S
authors.lastname: Yoon
authors.forename: Sungsoo
authors.initials: S
authors.lastname: Kim
authors.forename: Jongkook
authors.initials: J
authors.lastname: Moon
authors.forename: Yeonwoo
authors.initials: Y
authors.lastname: Ryu
authors.forename: Kyeong Kyu
authors.initials: KK
authors.lastname: Kim
authors.forename: T Doohun
authors.initials: TD
authors.lastname: Kim
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D020836:Protein Structure, Quaternary; D001618:beta-Lactamases / Q000737:chemistry* / Q000302:isolation & purification*
chemical_list: D001618:beta-Lactamases