Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Solving a new R2lox protein structure by microcrystal electron diffraction
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).ORCID iD: 0000-0002-5466-6508
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).
Show others and affiliations
Number of Authors: 72019 (English)In: Science Advances, E-ISSN 2375-2548, Vol. 5, no 8, article id eaax4621Article in journal (Refereed) Published
Abstract [en]

Microcrystal electron diffraction (MicroED) has recently shown potential for structural biology. It enables the study of biomolecules from micrometer-sized 3D crystals that are too small to be studied by conventional x-ray crystallography. However, to date, MicroED has only been applied to redetermine protein structures that had already been solved previously by x-ray diffraction. Here, we present the first new protein structure-an R2lox enzyme-solved using MicroED. The structure was phased by molecular replacement using a search model of 35% sequence identity. The resulting electrostatic scattering potential map at 3.0-angstrom resolution was of sufficient quality to allow accurate model building and refinement. The dinuclear metal cofactor could be located in the map and was modeled as a heterodinuclear Mn/Fe center based on previous studies. Our results demonstrate that MicroED has the potential to become a widely applicable tool for revealing novel insights into protein structure and function.

Place, publisher, year, edition, pages
2019. Vol. 5, no 8, article id eaax4621
National Category
Physical Sciences Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-173201DOI: 10.1126/sciadv.aax4621ISI: 000481798400057PubMedID: 31457106OAI: oai:DiVA.org:su-173201DiVA, id: diva2:1351756
Available from: 2019-09-16 Created: 2019-09-16 Last updated: 2019-09-16Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Xu, HongyiLebrette, HugoClabbers, Max T. B.Zhao, JingjingGriese, Julia J.Zou, XiaodongHögbom, Martin
By organisation
Department of Materials and Environmental Chemistry (MMK)Department of Biochemistry and Biophysics
In the same journal
Science Advances
Physical SciencesBiological Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 4 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf