Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae

Noella Silva-Martin; Rafael Molina; Ivan Angulo; José M Mancheño; Pedro García; Juan A Hermoso

doi:10.1107/S1744309110006718

Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae

Noella Silva-Martin, Rafael Molina, Ivan Angulo, José M Mancheño, Pedro García, Juan A Hermoso

Protein Structure and Function Program

8 Citationer (Scopus)

Abstract

As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl - 7 cleaves the glycosidic Β1,4 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 Å. Diffraction data sets were collected to 2.4 Å resolution using a rotating-anode generator.

Originalsprog	Engelsk
Tidsskrift	Acta Crystallographica Section F: Structural Biology Communications
Vol/bind	66
Udgave nummer	Pt 6
Sider (fra-til)	670-3
Antal sider	4
ISSN	2053-230X
DOI	https://doi.org/10.1107/S1744309110006718
Status	Udgivet - 1 jun. 2010

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10.1107/S1744309110006718

Citationsformater

Silva-Martin, N., Molina, R., Angulo, I., Mancheño, J. M., García, P., & Hermoso, J. A. (2010). Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae. Acta Crystallographica Section F: Structural Biology Communications, 66(Pt 6), 670-3. https://doi.org/10.1107/S1744309110006718

Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae. / Silva-Martin, Noella; Molina, Rafael; Angulo, Ivan et al.

I: Acta Crystallographica Section F: Structural Biology Communications, Bind 66, Nr. Pt 6, 01.06.2010, s. 670-3.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Silva-Martin, N, Molina, R, Angulo, I, Mancheño, JM, García, P & Hermoso, JA 2010, 'Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae', Acta Crystallographica Section F: Structural Biology Communications, bind 66, nr. Pt 6, s. 670-3. https://doi.org/10.1107/S1744309110006718

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title = "Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae",

abstract = "As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl - 7 cleaves the glycosidic Β1,4 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 {\AA}. Diffraction data sets were collected to 2.4 {\AA} resolution using a rotating-anode generator.",

keywords = "Bacteriophages/chemistry, Biocatalysis, Crystallization, Crystallography, X-Ray, Endopeptidases/chemistry, Streptococcus pneumoniae/virology",

author = "Noella Silva-Martin and Rafael Molina and Ivan Angulo and Manche{\~n}o, {Jos{\'e} M} and Pedro Garc{\'i}a and Hermoso, {Juan A}",

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T1 - Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae

AU - Silva-Martin, Noella

AU - Molina, Rafael

AU - Angulo, Ivan

AU - Mancheño, José M

AU - García, Pedro

AU - Hermoso, Juan A

PY - 2010/6/1

Y1 - 2010/6/1

N2 - As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl - 7 cleaves the glycosidic Β1,4 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 Å. Diffraction data sets were collected to 2.4 Å resolution using a rotating-anode generator.

AB - As part of the life cycle of the pneumococcal phage Cp-7, the endolysin Cpl - 7 cleaves the glycosidic Β1,4 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 Å. Diffraction data sets were collected to 2.4 Å resolution using a rotating-anode generator.

KW - Bacteriophages/chemistry

KW - Biocatalysis

KW - Crystallization

KW - Crystallography, X-Ray

KW - Endopeptidases/chemistry

KW - Streptococcus pneumoniae/virology

U2 - 10.1107/S1744309110006718

DO - 10.1107/S1744309110006718

M3 - Journal article

C2 - 20516596

SN - 2053-230X

VL - 66

SP - 670

EP - 673

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - Pt 6

ER -

Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae

Abstract

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