Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV)

Adeline Goulet; Silvia Spinelli; Valérie Campanacci; Sophie Porciero; Stéphanie Blangy; Roger A Garrett; Herman van Tilbeurgh; Nicolas Leulliot; Tamara Basta; David Prangishvili; Christian Cambillau

doi:10.1107/S1744309106029150

Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV)

Adeline Goulet, Silvia Spinelli, Valérie Campanacci, Sophie Porciero, Stéphanie Blangy, Roger A Garrett, Herman van Tilbeurgh, Nicolas Leulliot, Tamara Basta, David Prangishvili, Christian Cambillau

Functional Genomics

4 Citations (Scopus)

Abstract

A large-scale programme has been embarked upon aiming towards the structural determination of conserved proteins from viruses infecting hyperthermophilic archaea. Here, the crystallization of protein 14 from the archaeal virus SIFV is reported. This protein, which contains 111 residues (MW 13 465 Da), was cloned and expressed in Escherichia coli with an N-terminal His(6) tag and purified to homogeneity. The tag was subsequently cleaved and the protein was crystallized using PEG 1000 or PEG 4000 as a precipitant. Large crystals were obtained of the native and the selenomethionine-labelled protein using sitting drops of 100-300 nl. Crystals belong to space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 68.1, c = 132.4 A. Diffraction data were collected to a maximum acceptable resolution of 2.95 and 3.20 A for the SeMet-labelled and native protein, respectively.

Original language	English
Journal	Acta Crystallographica. Section F : Structural Biology and Crystallization Communications
Volume	62
Issue number	Pt 9
Pages (from-to)	884-886
Number of pages	2
ISSN	1744-3091
DOIs	https://doi.org/10.1107/S1744309106029150
Publication status	Published - 2006

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Goulet, A., Spinelli, S., Campanacci, V., Porciero, S., Blangy, S., Garrett, R. A., van Tilbeurgh, H., Leulliot, N., Basta, T., Prangishvili, D., & Cambillau, C. (2006). Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV). Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, 62(Pt 9), 884-886. https://doi.org/10.1107/S1744309106029150

Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV). / Goulet, Adeline; Spinelli, Silvia; Campanacci, Valérie et al.

In: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, Vol. 62, No. Pt 9, 2006, p. 884-886.

Research output: Contribution to journal › Journal article › Research › peer-review

Goulet, A, Spinelli, S, Campanacci, V, Porciero, S, Blangy, S, Garrett, RA, van Tilbeurgh, H, Leulliot, N, Basta, T, Prangishvili, D & Cambillau, C 2006, 'Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV)', Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, vol. 62, no. Pt 9, pp. 884-886. https://doi.org/10.1107/S1744309106029150

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title = "Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV)",

abstract = "A large-scale programme has been embarked upon aiming towards the structural determination of conserved proteins from viruses infecting hyperthermophilic archaea. Here, the crystallization of protein 14 from the archaeal virus SIFV is reported. This protein, which contains 111 residues (MW 13 465 Da), was cloned and expressed in Escherichia coli with an N-terminal His(6) tag and purified to homogeneity. The tag was subsequently cleaved and the protein was crystallized using PEG 1000 or PEG 4000 as a precipitant. Large crystals were obtained of the native and the selenomethionine-labelled protein using sitting drops of 100-300 nl. Crystals belong to space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 68.1, c = 132.4 A. Diffraction data were collected to a maximum acceptable resolution of 2.95 and 3.20 A for the SeMet-labelled and native protein, respectively.",

author = "Adeline Goulet and Silvia Spinelli and Val{\'e}rie Campanacci and Sophie Porciero and St{\'e}phanie Blangy and Garrett, {Roger A} and {van Tilbeurgh}, Herman and Nicolas Leulliot and Tamara Basta and David Prangishvili and Christian Cambillau",

note = "Keywords: Cloning, Molecular; Crystallization; Lipothrixviridae; Sulfolobus; Viral Proteins; X-Ray Diffraction",

year = "2006",

doi = "10.1107/S1744309106029150",

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T1 - Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV)

AU - Goulet, Adeline

AU - Spinelli, Silvia

AU - Campanacci, Valérie

AU - Porciero, Sophie

AU - Blangy, Stéphanie

AU - Garrett, Roger A

AU - van Tilbeurgh, Herman

AU - Leulliot, Nicolas

AU - Basta, Tamara

AU - Prangishvili, David

AU - Cambillau, Christian

N1 - Keywords: Cloning, Molecular; Crystallization; Lipothrixviridae; Sulfolobus; Viral Proteins; X-Ray Diffraction

PY - 2006

Y1 - 2006

N2 - A large-scale programme has been embarked upon aiming towards the structural determination of conserved proteins from viruses infecting hyperthermophilic archaea. Here, the crystallization of protein 14 from the archaeal virus SIFV is reported. This protein, which contains 111 residues (MW 13 465 Da), was cloned and expressed in Escherichia coli with an N-terminal His(6) tag and purified to homogeneity. The tag was subsequently cleaved and the protein was crystallized using PEG 1000 or PEG 4000 as a precipitant. Large crystals were obtained of the native and the selenomethionine-labelled protein using sitting drops of 100-300 nl. Crystals belong to space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 68.1, c = 132.4 A. Diffraction data were collected to a maximum acceptable resolution of 2.95 and 3.20 A for the SeMet-labelled and native protein, respectively.

AB - A large-scale programme has been embarked upon aiming towards the structural determination of conserved proteins from viruses infecting hyperthermophilic archaea. Here, the crystallization of protein 14 from the archaeal virus SIFV is reported. This protein, which contains 111 residues (MW 13 465 Da), was cloned and expressed in Escherichia coli with an N-terminal His(6) tag and purified to homogeneity. The tag was subsequently cleaved and the protein was crystallized using PEG 1000 or PEG 4000 as a precipitant. Large crystals were obtained of the native and the selenomethionine-labelled protein using sitting drops of 100-300 nl. Crystals belong to space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 68.1, c = 132.4 A. Diffraction data were collected to a maximum acceptable resolution of 2.95 and 3.20 A for the SeMet-labelled and native protein, respectively.

U2 - 10.1107/S1744309106029150

DO - 10.1107/S1744309106029150

M3 - Journal article

C2 - 16946470

SN - 2053-230X

VL - 62

SP - 884

EP - 886

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - Pt 9

ER -

Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV)

Abstract

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