A strategy for dissecting the architectures of native macromolecular assemblies.

Shi, Yi; Pellarin, Riccardo; Fridy, Peter C; Fernandez-Martinez, Javier; Thompson, Mary K; Li, Yinyin; Wang, Qing Jun; Sali, Andrej; Rout, Michael P; Chait, Brian T

Shi, Yi; Pellarin, Riccardo; Fridy, Peter C; Fernandez-Martinez, Javier; Thompson, Mary K; Li, Yinyin; Wang, Qing Jun; Sali, Andrej; Rout, Michael P; Chait, Brian T.

Afiliação

Shi Y; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York, USA.
Pellarin R; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California, USA.
Fridy PC; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, USA.
Fernandez-Martinez J; California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, California, USA.
Thompson MK; Institut Pasteur, Paris, France.
Li Y; Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York, USA.
Wang QJ; Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York, USA.
Sali A; Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York, USA.
Rout MP; Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York, USA.

Nat Methods ; 12(12): 1135-8, 2015 Dec.

Article em En | MEDLINE | ID: mdl-26436480

ABSTRACT

ABSTRACT

It remains particularly problematic to define the structures of native macromolecular assemblies, which are often of low abundance. Here we present a strategy for isolating complexes at endogenous levels from GFP-tagged transgenic cell lines. Using cross-linking mass spectrometry, we extracted distance restraints that allowed us to model the complexes' molecular architectures.

Assuntos

Espectrometria de Massas/métodos; Modelos Moleculares; Complexos Multiproteicos/química; Conformação Proteica; Animais; Reagentes de Ligações Cruzadas/química; Eletroforese em Gel de Poliacrilamida; Exossomos/química; Proteínas de Fluorescência Verde/genética; Fígado/química; Camundongos Transgênicos; Complexos Multiproteicos/genética; Saccharomyces cerevisiae/química; Proteínas de Saccharomyces cerevisiae/química; Sensibilidade e Especificidade

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Conformação Proteica / Espectrometria de Massas / Modelos Moleculares / Complexos Multiproteicos Tipo de estudo: Diagnostic_studies Limite: Animals Idioma: En Revista: Nat Methods Assunto da revista: TECNICAS E PROCEDIMENTOS DE LABORATORIO Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Estados Unidos

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