Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp‐7, a phage infecting Streptococcus pneumoniae
As part of the life cycle of the pneumococcal phage Cp‐7, the endolysin Cpl‐7 cleaves the glycosidic β1,4 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 Å. Diffraction data sets were collected to 2.4 Å resolution using a rotating‐anode generator.
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