Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infecting Streptococcus pneumoniae.
Endolysin from the phage Cp-1 (Cpl-1) cleaves the glycosidic beta1,4-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 C222(1), with unit-cell parameters a = 77.949, b = 95.782, c = 129.282 A. Diffraction data to a resolution of 2.1 A were collected at a synchrotron facility.
Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Begoña
B
Monterroso
Armando
A
Albert
Martín
M
Martínez-Ripoll
Pedro
P
García
José Luis
JL
García
Margarita
M
Menéndez
Juan A
JA
Hermoso
D003460:Crystallization; D018360:Crystallography, X-Ray; D009113:Muramidase / Q000737:chemistry*; D017108:Streptococcus Phages / Q000201:enzymology*; D013296:Streptococcus pneumoniae / Q000821:virology*
D009113:Muramidase