Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV

Adeline Goulet; Gisle Alberg Vestergaard; Catarina Felisberto-Rodrigues; Valérie Campanacci; Roger Antony Garrett; Christian Cambillau; Miguel Ortiz-Lombardía

doi:10.1107/s0907444909051798

Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV

Adeline Goulet, Gisle Alberg Vestergaard, Catarina Felisberto-Rodrigues, Valérie Campanacci, Roger Antony Garrett, Christian Cambillau, Miguel Ortiz-Lombardía

34 Citations (Scopus)

Abstract

The structure of a 14 kDa structural protein from Acidianus two-tailed virus (ATV) was solved by single-wavelength anomalous diffraction (SAD) phasing using X-ray data collected at 2.0 Å wavelength. Although the anomalous signal from methionine sulfurs was expected to suffice to solve the structure, one chloride ion turned out to be essential to achieve phasing. The minimal data requirements and the relative contributions of the Cl and S atoms to phasing are discussed. This work supports the feasibility of a systematic approach for the solution of protein crystal structures by SAD based on intrinsic protein light atoms along with associated chloride ions from the solvent. In such cases, data collection at long wavelengths may be a time-efficient alternative to seleno-methionine substitution and heavy-atom derivatization.

Original language	English
Journal	Acta Crystallographica. Section D: Biological Crystallography
Volume	66
Issue number	Pt 3
Pages (from-to)	304-308
Number of pages	5
ISSN	0907-4449
DOIs	https://doi.org/10.1107/s0907444909051798
Publication status	Published - 12 Feb 2010

Keywords

Acidianus
Chlorine
Crystallography, X-Ray
Models, Molecular
Protein Structure, Tertiary
Selenomethionine
Sulfur
Viral Structural Proteins
X-Rays

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Goulet, A., Vestergaard, G. A., Felisberto-Rodrigues, C., Campanacci, V., Garrett, R. A., Cambillau, C., & Ortiz-Lombardía, M. (2010). Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV. Acta Crystallographica. Section D: Biological Crystallography, 66(Pt 3), 304-308. https://doi.org/10.1107/s0907444909051798

Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV. / Goulet, Adeline; Vestergaard, Gisle Alberg; Felisberto-Rodrigues, Catarina et al.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 66, No. Pt 3, 12.02.2010, p. 304-308.

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

Goulet, A, Vestergaard, GA, Felisberto-Rodrigues, C, Campanacci, V, Garrett, RA, Cambillau, C & Ortiz-Lombardía, M 2010, 'Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV', Acta Crystallographica. Section D: Biological Crystallography, vol. 66, no. Pt 3, pp. 304-308. https://doi.org/10.1107/s0907444909051798

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title = "Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV",

abstract = "The structure of a 14 kDa structural protein from Acidianus two-tailed virus (ATV) was solved by single-wavelength anomalous diffraction (SAD) phasing using X-ray data collected at 2.0 {\AA} wavelength. Although the anomalous signal from methionine sulfurs was expected to suffice to solve the structure, one chloride ion turned out to be essential to achieve phasing. The minimal data requirements and the relative contributions of the Cl and S atoms to phasing are discussed. This work supports the feasibility of a systematic approach for the solution of protein crystal structures by SAD based on intrinsic protein light atoms along with associated chloride ions from the solvent. In such cases, data collection at long wavelengths may be a time-efficient alternative to seleno-methionine substitution and heavy-atom derivatization.",

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AU - Felisberto-Rodrigues, Catarina

AU - Campanacci, Valérie

AU - Garrett, Roger Antony

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AB - The structure of a 14 kDa structural protein from Acidianus two-tailed virus (ATV) was solved by single-wavelength anomalous diffraction (SAD) phasing using X-ray data collected at 2.0 Å wavelength. Although the anomalous signal from methionine sulfurs was expected to suffice to solve the structure, one chloride ion turned out to be essential to achieve phasing. The minimal data requirements and the relative contributions of the Cl and S atoms to phasing are discussed. This work supports the feasibility of a systematic approach for the solution of protein crystal structures by SAD based on intrinsic protein light atoms along with associated chloride ions from the solvent. In such cases, data collection at long wavelengths may be a time-efficient alternative to seleno-methionine substitution and heavy-atom derivatization.

KW - Acidianus

KW - Chlorine

KW - Crystallography, X-Ray

KW - Models, Molecular

KW - Protein Structure, Tertiary

KW - Selenomethionine

KW - Sulfur

KW - Viral Structural Proteins

KW - X-Rays

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JO - Acta Crystallographica Section D: Structural Biology

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IS - Pt 3

ER -

Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV

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Keywords

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