Purification, crystallization and preliminary crystallographic analysis of Est-Y29: a novel oligomeric beta-lactamase.
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.
Kim
Seungbum
S
Department of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
Joo
Sangbum
S
Yoon
Sangyoung
S
Kim
Sungsoo
S
Moon
Jongkook
J
Ryu
Yeonwoo
Y
Kim
Kyeong Kyu
KK
Kim
T Doohun
TD
D003460:Crystallization; D018360:Crystallography, X-Ray; D020836:Protein Structure, Quaternary; D001618:beta-Lactamases / Q000737:chemistry* / Q000302:isolation & purification*
D001618:beta-Lactamases