Acta Crystallographica Section D

Biological Crystallography

Volume 58, Part 9 (September 2002)

crystallization papers

Acta Cryst. (2002). D58, 1487-1489 [ doi:10.1107/S0907444902011563 ]

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

B. Monterroso, A. Albert, M. Martínez-Ripoll, P. García, J. L. García, M. Menéndez and J. A. Hermoso

Abstract: Endolysin from the phage Cp-1 (Cpl-1) cleaves the glycosidic [beta] 1,4-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- [beta] -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.

Keywords: Cpl-1 lysozyme; endolysin.