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TitleGeneral and robust covalently linked graphene oxide affinity grids for high-resolution cryo-EM.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 39, Page 24269-24273, Year 2020
Publish dateSep 29, 2020
AuthorsFeng Wang / Yanxin Liu / Zanlin Yu / Sam Li / Shengjie Feng / Yifan Cheng / David A Agard /
PubMed AbstractAffinity grids have great potential to facilitate rapid preparation of even quite impure samples in single-particle cryo-electron microscopy (EM). Yet despite the promising advances of affinity grids ...Affinity grids have great potential to facilitate rapid preparation of even quite impure samples in single-particle cryo-electron microscopy (EM). Yet despite the promising advances of affinity grids over the past decades, no single strategy has demonstrated general utility. Here we chemically functionalize cryo-EM grids coated with mostly one or two layers of graphene oxide to facilitate affinity capture. The protein of interest is tagged using a system that rapidly forms a highly specific covalent bond to its cognate catcher linked to the grid via a polyethylene glycol (PEG) spacer. Importantly, the spacer keeps particles away from both the air-water interface and the graphene oxide surface, protecting them from potential denaturation and rendering them sufficiently flexible to avoid preferential sample orientation concerns. Furthermore, the PEG spacer successfully reduces nonspecific binding, enabling high-resolution reconstructions from a much cruder lysate sample.
External linksProc Natl Acad Sci U S A / PubMed:32913054 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.42 Å
Structure data

22174

6xg6

EMDB-22174, PDB-6xg6:
Full-length human mitochondrial Hsp90 (TRAP1) with ADP-BeF3
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-22175:
Human mitochondrial Hsp90 (TRAP1) NTD-Middle domain dimer with ADP-BeF3
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-22176:
Full-length human mitochondrial Hsp90 (TRAP1) with ADP-BeF3
Method: EM (single particle) / Resolution: 4.42 Å

EMDB-22177:
Human mitochondrial Hsp90 (TRAP1) NTD-Middle domain dimer with ADP-BeF3
Method: EM (single particle) / Resolution: 4.11 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

Source
  • homo sapiens (human)
  • streptococcus pyogenes (bacteria)
KeywordsCHAPERONE / Hsp90

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