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Título: | Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infecting Streptococcus pneumoniae |
Autor: | Monterroso, Begoña CSIC ORCID ; Albert, Armando CSIC ORCID; Martínez-Ripoll, Martín CSIC ORCID; García, Pedro CSIC ORCID ; García, José Luis CSIC ORCID ; Menéndez, Margarita CSIC ORCID; Hermoso, Juan A. CSIC ORCID | Palabras clave: | Cpl-1 lysozyme Endolysin |
Fecha de publicación: | sep-2002 | Editor: | International Union of Crystallography | Citación: | Acta Crystallographica - Section D-Biological Crystallography 58(Pt 9) 1487-9 (2002) | Resumen: | 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. | Descripción: | 3 p.-2 fig.-1 tab. | Versión del editor: | https://doi.org/10.1107/S0907444902011563 | URI: | http://hdl.handle.net/10261/242076 | DOI: | 10.1107/S0907444902011563 | E-ISSN: | 2059-7983 |
Aparece en las colecciones: | (CIB) Artículos |
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