Open AccessCrystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp‐7, a phage infecting Streptococcus pneumoniae
Author(s) -
SilvaMartin Noella,
Molina Rafael,
Angulo Ivan,
Mancheño José M.,
García Pedro,
Hermoso Juan A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110006718
Subject(s) - lysin , streptococcus pneumoniae , crystallization , crystallography , microbiology and biotechnology , bacteriophage , chemistry , materials science , biology , biochemistry , organic chemistry , gene , antibiotics , escherichia coli
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 I 422, 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.