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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Standard

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; Campanacci, Valérie; Garrett, Roger Antony; Cambillau, Christian; Ortiz-Lombardía, Miguel.

I: Acta Crystallographica. Section D: Biological Crystallography, Bind 66, Nr. Pt 3, 2010, s. 304-308.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

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, bind 66, nr. Pt 3, s. 304-308. https://doi.org/10.1107/S0907444909051798

APA

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

Vancouver

Goulet A, Vestergaard GA, Felisberto-Rodrigues C, Campanacci V, Garrett RA, Cambillau C o.a. 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. 2010;66(Pt 3):304-308. https://doi.org/10.1107/S0907444909051798

Author

Goulet, Adeline ; Vestergaard, Gisle Alberg ; Felisberto-Rodrigues, Catarina ; Campanacci, Valérie ; Garrett, Roger Antony ; Cambillau, Christian ; Ortiz-Lombardía, Miguel. / Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV. I: Acta Crystallographica. Section D: Biological Crystallography. 2010 ; Bind 66, Nr. Pt 3. s. 304-308.

Bibtex

@article{0c082f334c65461684fc054b9cb4cb29,
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 A 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 selenomethionine substitution and heavy-atom derivatization.",
keywords = "Acidianus, Chlorine, Crystallography, X-Ray, Models, Molecular, Protein Structure, Tertiary, Selenomethionine, Sulfur, Viral Structural Proteins, X-Rays",
author = "Adeline Goulet and Vestergaard, {Gisle Alberg} and Catarina Felisberto-Rodrigues and Val{\'e}rie Campanacci and Garrett, {Roger Antony} and Christian Cambillau and Miguel Ortiz-Lombard{\'i}a",
year = "2010",
doi = "10.1107/S0907444909051798",
language = "English",
volume = "66",
pages = "304--308",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "Pt 3",

}

RIS

TY - JOUR

T1 - Getting the best out of long-wavelength X-rays: de novo chlorine/sulfur SAD phasing of a structural protein from ATV

AU - Goulet, Adeline

AU - Vestergaard, Gisle Alberg

AU - Felisberto-Rodrigues, Catarina

AU - Campanacci, Valérie

AU - Garrett, Roger Antony

AU - Cambillau, Christian

AU - Ortiz-Lombardía, Miguel

PY - 2010

Y1 - 2010

N2 - 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 A 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 selenomethionine substitution and heavy-atom derivatization.

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 A 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 selenomethionine 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

U2 - 10.1107/S0907444909051798

DO - 10.1107/S0907444909051798

M3 - Journal article

C2 - 20179342

VL - 66

SP - 304

EP - 308

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - Pt 3

ER -

ID: 33493878