2024-03-29T02:27:18Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1081732021-12-28T16:18:51Zcom_10261_86com_10261_1col_10261_339
Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae
Silva-Martín, Noella
Molina, Rafael
Angulo, Iván
Mancheño, Jose M.
García, Pedro
Hermoso, Juan A.
4 p.-4 fig.-1 tab.
As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl-7 cleaves the glycosidic 1,4 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 I422, with unit-cell parameters a = 127.93, b = 127.93, c = 82.07 A˚ . Diffraction data sets were collected to 2.4 A˚ resolution using a rotating-anode generator.
This work was supported by grants from the Spanish Ministry of Science and Technology (BFU2008-01711, SAF2006-00390), EUCP223111
(CAREPNEUMO, European Union), the COMBACT
program (S-BIO-0260/2006) and CIBER de Enfermedades Respiratorias
(CIBERES)
Peer reviewed
2014-11-28T09:42:55Z
2014-11-28T09:42:55Z
2010-06-01
artículo
http://purl.org/coar/resource_type/c_6501
Acta Cryst. F (2010) 66 (6) 670–673
1744-3091
http://hdl.handle.net/10261/108173
10.1107/S1744309110006718
20516596
en
Publisher's version
http://dx.doi.org/10.1107/S1744309110006718
Sí
open
International Union of Crystallography