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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.

SUBMITTER: Kim S

PROVIDER: S-EPMC2650449 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary crystallographic analysis of Est-Y29: a novel oligomeric beta-lactamase.

Kim Seungbum S Joo Sangbum S Yoon Sangyoung S Kim Sungsoo S Moon Jongkook J Ryu Yeonwoo Y Kim Kyeong Kyu KK Kim T Doohun TD

Acta crystallographica. Section F, Structural biology and crystallization communications 20090226 Pt 3

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 t ...[more]

PMID: 19255492

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