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Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae.

ABSTRACT: As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl-7 cleaves the glycosidic beta1,4 bonds between N-acetylmuramic acid and N-acetylglucosamine in the pneumococcal cell wall, resulting in bacterial lysis. Recombinant Cpl-7 was overexpressed in Escherichia coli, purified and crystallized using the vapour-diffusion method at 291 K. Diffraction-quality tetragonal crystals of the catalytic module of Cpl-7 were obtained from a mixture of PEG 3350 and sodium formate. The crystals belonged to space group I422, with unit-cell parameters a = 127.93, b = 127.93, c = 82.07 A. Diffraction data sets were collected to 2.4 A resolution using a rotating-anode generator.

SUBMITTER: Silva-Martin N

PROVIDER: S-EPMC2882766 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae.

Silva-Martin Noella N Molina Rafael R Angulo Ivan I Mancheño José M JM García Pedro P Hermoso Juan A JA

Acta crystallographica. Section F, Structural biology and crystallization communications 20100526 Pt 6

As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl-7 cleaves the glycosidic beta1,4 bonds between N-acetylmuramic acid and N-acetylglucosamine in the pneumococcal cell wall, resulting in bacterial lysis. Recombinant Cpl-7 was overexpressed in Escherichia coli, purified and crystallized using the vapour-diffusion method at 291 K. Diffraction-quality tetragonal crystals of the catalytic module of Cpl-7 were obtained from a mixture of PEG 3350 and sodium formate. The crysta ...[more]

PMID: 20516596

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