Journal
SCIENCE ADVANCES
Volume 5, Issue 8, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aax4621
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Funding
- Knut and Alice Wallenberg Foundation [2012.0112, 2017.0275]
- Science for Life Laboratory through the pilot project grant Electron Nanocrystallography
- European Research Council (HIGH-GEAR) [724394]
- Swedish Research Council [2017-04018, 2017-05333]
- Swedish Research Council [2017-04018] Funding Source: Swedish Research Council
- European Research Council (ERC) [724394] Funding Source: European Research Council (ERC)
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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.
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