Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infectingStreptococcus pneumoniae

Endolysin from the phage Cp-1 (Cpl-1) cleaves the glycosidic β1,4-­bonds between the N-acetylmuramic acid and the N-­acetylglucosamine of the pneumococcal cell wall. Cpl-1 has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality orthorhombic crystals of the native protein were obtained only after addition of the detergent n-decyl-β-­d-­maltoside. Crystals belong to space group C2221, with unit-cell parameters a = 77.949, b = 95.782, c = 129.282 Å. Diffraction data to a resolution of 2.1 Å were collected at a synchrotron facility.