Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Cryo-EM structure of haemoglobin at 3.2 angstrom determined with the Volta phase plate

Khoshouei, M., Radjainia, M., Baumeister, W., & Danev, R. (2017). Cryo-EM structure of haemoglobin at 3.2 angstrom determined with the Volta phase plate. Nature Communications, 8: 16099. doi:10.1038/ncomms16099.

Item is

Dateien

einblenden: Dateien
ausblenden: Dateien
:
ncomms16099.pdf (Verlagsversion), 4MB
Name:
ncomms16099.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
Open Access This article is licensed under a Creative Commons Attribution 4.0 International License.
Lizenz:
-

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Khoshouei, Maryam1, Autor           
Radjainia, Mazdak2, Autor
Baumeister, Wolfgang1, Autor           
Danev, Radostin1, Autor           
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

Inhalt

einblenden:
ausblenden:
Schlagwörter: ELECTRON-MICROSCOPY; CRYOELECTRON MICROSCOPY; CRYSTAL-STRUCTURES; RESOLUTION; REFINEMENTScience & Technology - Other Topics;
 Zusammenfassung: With the advent of direct electron detectors, the perspectives of cryo-electron microscopy (cryo-EM) have changed in a profound way. These cameras are superior to previous detectors in coping with the intrinsically low contrast and beam-induced motion of radiation-sensitive organic materials embedded in amorphous ice, and hence they have enabled the structure determination of many macromolecular assemblies to atomic or near-atomic resolution. Nevertheless, there are still limitations and one of them is the size of the target structure. Here, we report the use of a Volta phase plate in determining the structure of human haemoglobin (64 kDa) at 3.2 angstrom. Our results demonstrate that this method can be applied to complexes that are significantly smaller than those previously studied by conventional defocus-based approaches. Cryo-EM is now close to becoming a fast and cost-effective alternative to crystallography for high-resolution protein structure determination.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2017-06-30
 Publikationsstatus: Online veröffentlicht
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000404455700001
DOI: 10.1038/ncomms16099
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Nature Communications
  Kurztitel : Nat. Commun.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: London : Nature Publishing Group
Seiten: - Band / Heft: 8 Artikelnummer: 16099 Start- / Endseite: - Identifikator: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723