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-Structure paper
Title | Solving a new R2lox protein structure by microcrystal electron diffraction. |
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Journal, issue, pages | Sci Adv, Vol. 5, Issue 8, Page eaax4621, Year 2019 |
Publish date | Aug 7, 2019 |
Authors | Hongyi Xu / Hugo Lebrette / Max T B Clabbers / Jingjing Zhao / Julia J Griese / Xiaodong Zou / Martin Högbom / |
PubMed Abstract | 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 ...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. |
External links | Sci Adv / PubMed:31457106 / PubMed Central |
Methods | EM (electron crystallography) |
Resolution | 3 Å |
Structure data | PDB-6qrz: |
Chemicals | ChemComp-MN3: ChemComp-FE: |
Source |
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Keywords | OXIDOREDUCTASE / micro-crystal / microED / R2-LIKE LIGAND-BINDING OXIDASE / MN/FE COFACTOR / RIBONUCLEOTIDE REDUCTASE R2 SUBUNIT FOLD / METALLOPROTEIN OXIDOREDUCTASE / FERRITIN-LIKE SUPERFAMILY |