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Revisiting the Structure of Hemoglobin and Myoglobin with Cryo-Electron Microscopy.
Khoshouei, Maryam; Danev, Radostin; Plitzko, Juergen M; Baumeister, Wolfgang.
Afiliación
  • Khoshouei M; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany.
  • Danev R; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany.
  • Plitzko JM; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany.
  • Baumeister W; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany. Electronic address: baumeist@biochem.mpg.de.
J Mol Biol ; 429(17): 2611-2618, 2017 08 18.
Article en En | MEDLINE | ID: mdl-28697886
ABSTRACT
Sixty years ago, the first protein structure of myoglobin was determined by John Kendrew and his colleagues; hemoglobin followed shortly thereafter. For quite some time, it seemed that only X-ray crystallography would be capable of determining the structure of proteins to high resolution. In recent years, cryo-electron microscopy has emerged as a viable alternative and indeed in many cases the preferred approach. It is capable of studying proteins that span a size range from several megadaltons to proteins as small as myoglobin and hemoglobin.
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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Hemoglobinas / Microscopía por Crioelectrón / Mioglobina Idioma: En Revista: J Mol Biol Año: 2017 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Hemoglobinas / Microscopía por Crioelectrón / Mioglobina Idioma: En Revista: J Mol Biol Año: 2017 Tipo del documento: Article País de afiliación: Alemania