Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA

Research output: Contribution to journalJournal articlepeer-review

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Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA. / Redondo, Pilar; Merino, Nekane; Villate, Maider; Blanco, Francisco J; Montoya, Guillermo; Molina, Rafael.

In: Acta crystallographica. Section F, Structural biology communications, Vol. 70, No. Pt 2, 02.2014, p. 256-9.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Redondo, P, Merino, N, Villate, M, Blanco, FJ, Montoya, G & Molina, R 2014, 'Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA', Acta crystallographica. Section F, Structural biology communications, vol. 70, no. Pt 2, pp. 256-9. https://doi.org/10.1107/S2053230X1400065X

APA

Redondo, P., Merino, N., Villate, M., Blanco, F. J., Montoya, G., & Molina, R. (2014). Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA. Acta crystallographica. Section F, Structural biology communications, 70(Pt 2), 256-9. https://doi.org/10.1107/S2053230X1400065X

Vancouver

Redondo P, Merino N, Villate M, Blanco FJ, Montoya G, Molina R. Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA. Acta crystallographica. Section F, Structural biology communications. 2014 Feb;70(Pt 2):256-9. https://doi.org/10.1107/S2053230X1400065X

Author

Redondo, Pilar ; Merino, Nekane ; Villate, Maider ; Blanco, Francisco J ; Montoya, Guillermo ; Molina, Rafael. / Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA. In: Acta crystallographica. Section F, Structural biology communications. 2014 ; Vol. 70, No. Pt 2. pp. 256-9.

Bibtex

@article{71bc595674c6439b96feae3d46a84eca,
title = "Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA",
abstract = "Homing endonucleases are highly specific DNA-cleaving enzymes that recognize long stretches of DNA. The engineering of these enzymes provides novel instruments for genome modification in a wide range of fields, including gene targeting, by inducing specific double-strand breaks. I-CvuI is a homing endonuclease from the green alga Chlorella vulgaris. This enzyme was purified after overexpression in Escherichia coli. Crystallization experiments of I-CvuI in complex with its DNA target in the presence of Mg(2+) yielded crystals suitable for X-ray diffraction analysis. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 62.83, b = 83.56, c = 94.40 {\AA}. The self-rotation function and the Matthews coefficient suggested the presence of one protein-DNA complex per asymmetric unit. The crystals diffracted to a resolution limit of 1.9 {\AA} using synchrotron radiation.",
keywords = "Chlorella vulgaris/enzymology, Chromatography, Liquid, Crystallization, Crystallography, X-Ray/methods, DNA/metabolism, Electrophoresis, Polyacrylamide Gel, Endonucleases/chemistry, Protein Conformation",
author = "Pilar Redondo and Nekane Merino and Maider Villate and Blanco, {Francisco J} and Guillermo Montoya and Rafael Molina",
year = "2014",
month = feb,
doi = "10.1107/S2053230X1400065X",
language = "English",
volume = "70",
pages = "256--9",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "Pt 2",

}

RIS

TY - JOUR

T1 - Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA

AU - Redondo, Pilar

AU - Merino, Nekane

AU - Villate, Maider

AU - Blanco, Francisco J

AU - Montoya, Guillermo

AU - Molina, Rafael

PY - 2014/2

Y1 - 2014/2

N2 - Homing endonucleases are highly specific DNA-cleaving enzymes that recognize long stretches of DNA. The engineering of these enzymes provides novel instruments for genome modification in a wide range of fields, including gene targeting, by inducing specific double-strand breaks. I-CvuI is a homing endonuclease from the green alga Chlorella vulgaris. This enzyme was purified after overexpression in Escherichia coli. Crystallization experiments of I-CvuI in complex with its DNA target in the presence of Mg(2+) yielded crystals suitable for X-ray diffraction analysis. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 62.83, b = 83.56, c = 94.40 Å. The self-rotation function and the Matthews coefficient suggested the presence of one protein-DNA complex per asymmetric unit. The crystals diffracted to a resolution limit of 1.9 Å using synchrotron radiation.

AB - Homing endonucleases are highly specific DNA-cleaving enzymes that recognize long stretches of DNA. The engineering of these enzymes provides novel instruments for genome modification in a wide range of fields, including gene targeting, by inducing specific double-strand breaks. I-CvuI is a homing endonuclease from the green alga Chlorella vulgaris. This enzyme was purified after overexpression in Escherichia coli. Crystallization experiments of I-CvuI in complex with its DNA target in the presence of Mg(2+) yielded crystals suitable for X-ray diffraction analysis. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 62.83, b = 83.56, c = 94.40 Å. The self-rotation function and the Matthews coefficient suggested the presence of one protein-DNA complex per asymmetric unit. The crystals diffracted to a resolution limit of 1.9 Å using synchrotron radiation.

KW - Chlorella vulgaris/enzymology

KW - Chromatography, Liquid

KW - Crystallization

KW - Crystallography, X-Ray/methods

KW - DNA/metabolism

KW - Electrophoresis, Polyacrylamide Gel

KW - Endonucleases/chemistry

KW - Protein Conformation

U2 - 10.1107/S2053230X1400065X

DO - 10.1107/S2053230X1400065X

M3 - Journal article

C2 - 24637769

VL - 70

SP - 256

EP - 259

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - Pt 2

ER -

ID: 203018884