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Solving a new R2lox protein structure by microcrystal electron diffraction
Stockholm University.
Stockholm University.
Stockholm University.
Stockholm University.
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2019 (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-Å 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
Structural Biology
Identifiers
URN: urn:nbn:se:uu:diva-390270DOI: 10.1126/sciadv.aax4621ISI: 000481798400057PubMedID: 31457106OAI: oai:DiVA.org:uu-390270DiVA, id: diva2:1341236
Funder
EU, European Research Council, 724394Knut and Alice Wallenberg Foundation, 2012.0112Knut and Alice Wallenberg Foundation, 2017.0275Science for Life Laboratory - a national resource center for high-throughput molecular bioscienceSwedish Research Council, 2017-04018Swedish Research Council, 2017-05333Available from: 2019-08-08 Created: 2019-08-08 Last updated: 2019-09-30Bibliographically approved

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