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Fast native-SAD phasing for routine macromolecular structure determination.
Weinert, Tobias; Olieric, Vincent; Waltersperger, Sandro; Panepucci, Ezequiel; Chen, Lirong; Zhang, Hua; Zhou, Dayong; Rose, John; Ebihara, Akio; Kuramitsu, Seiki; Li, Dianfan; Howe, Nicole; Schnapp, Gisela; Pautsch, Alexander; Bargsten, Katja; Prota, Andrea E; Surana, Parag; Kottur, Jithesh; Nair, Deepak T; Basilico, Federica; Cecatiello, Valentina; Pasqualato, Sebastiano; Boland, Andreas; Weichenrieder, Oliver; Wang, Bi-Cheng; Steinmetz, Michel O; Caffrey, Martin; Wang, Meitian.
Afiliação
  • Weinert T; Swiss Light Source at Paul Scherrer Institut, Villigen, Switzerland.
  • Olieric V; Swiss Light Source at Paul Scherrer Institut, Villigen, Switzerland.
  • Waltersperger S; Swiss Light Source at Paul Scherrer Institut, Villigen, Switzerland.
  • Panepucci E; Swiss Light Source at Paul Scherrer Institut, Villigen, Switzerland.
  • Chen L; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.
  • Zhang H; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.
  • Zhou D; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.
  • Rose J; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.
  • Ebihara A; Laboratory of Biological Chemistry, Faculty of Applied Biological Sciences, Gifu University, Gifu, Japan.
  • Kuramitsu S; Department of Biological Sciences, Graduate School of Science, Osaka University, Osaka, Japan.
  • Li D; Membrane Structural and Functional Biology Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.
  • Howe N; Membrane Structural and Functional Biology Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.
  • Schnapp G; Boehringer Ingelheim Pharma GmbH and Co. KG, Biberach an der Riss, Germany.
  • Pautsch A; Boehringer Ingelheim Pharma GmbH and Co. KG, Biberach an der Riss, Germany.
  • Bargsten K; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.
  • Prota AE; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.
  • Surana P; National Centre for Biological Sciences, Bangalore, India.
  • Kottur J; National Centre for Biological Sciences, Bangalore, India.
  • Nair DT; National Centre for Biological Sciences, Bangalore, India.
  • Basilico F; Department of Experimental Oncology, European Institute of Oncology, Milan, Italy.
  • Cecatiello V; Department of Experimental Oncology, European Institute of Oncology, Milan, Italy.
  • Pasqualato S; Department of Experimental Oncology, European Institute of Oncology, Milan, Italy.
  • Boland A; Department of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.
  • Weichenrieder O; Department of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.
  • Wang BC; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA.
  • Steinmetz MO; Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.
  • Caffrey M; Membrane Structural and Functional Biology Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.
  • Wang M; Swiss Light Source at Paul Scherrer Institut, Villigen, Switzerland.
Nat Methods ; 12(2): 131-3, 2015 Feb.
Article em En | MEDLINE | ID: mdl-25506719
ABSTRACT
We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Difração de Raios X / Complexos Multiproteicos / Proteínas de Ligação a DNA / Proteínas de Membrana Limite: Animals / Humans Idioma: En Ano de publicação: 2015 Tipo de documento: Article
Texto completo
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PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Difração de Raios X / Complexos Multiproteicos / Proteínas de Ligação a DNA / Proteínas de Membrana Limite: Animals / Humans Idioma: En Ano de publicação: 2015 Tipo de documento: Article