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Solving a new R2lox...
Solving a new R2lox protein structure by microcrystal electron diffraction
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- Xu, Hongyi (författare)
- Stockholms universitet,Institutionen för material- och miljökemi (MMK),Stockholm University
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- Lebrette, Hugo (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
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- Clabbers, Max T. B. (författare)
- Stockholms universitet,Institutionen för material- och miljökemi (MMK),Stockholm University
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- Zhao, Jingjing (författare)
- Stockholms universitet,Institutionen för material- och miljökemi (MMK),Stockholm University
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- Griese, Julia J. (författare)
- Uppsala universitet,Stockholms universitet,Institutionen för biokemi och biofysik,Uppsala University, Sweden,Strukturbiologi,Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
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- Zou, Xiaodong (författare)
- Stockholms universitet,Institutionen för material- och miljökemi (MMK),Stockholm University
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- Högbom, Martin (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
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(creator_code:org_t)
- American Association for the Advancement of Science (AAAS), 2019
- 2019
- Engelska.
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Ingår i: Science Advances. - : American Association for the Advancement of Science (AAAS). - 2375-2548. ; 5:8
- Relaterad länk:
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https://doi.org/10.1...
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https://advances.sci...
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https://uu.diva-port... (primary) (Raw object)
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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