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TitleImproving particle quality in cryo-EM analysis using a PEGylation method.
Journal, issue, pagesStructure, Vol. 29, Issue 10, Page 1192-11199.e4, Year 2021
Publish dateOct 7, 2021
AuthorsZhikuan Zhang / Hideki Shigematsu / Toshiyuki Shimizu / Umeharu Ohto /
PubMed AbstractCryo-electron microscopy (cryo-EM) is widely used for structural biology studies and has been developed extensively in recent years. However, its sample vitrification process is a major limitation ...Cryo-electron microscopy (cryo-EM) is widely used for structural biology studies and has been developed extensively in recent years. However, its sample vitrification process is a major limitation because it causes severe particle aggregation and/or denaturation. This effect is thought to occur because particles tend to stick to the "deadly" air-water interface during vitrification. Here, we report a method for PEGylation of proteins that can efficiently protect particles against such problems during vitrification. This method alleviates the laborious process of fine-tuning the vitrification conditions, allowing for analysis of samples that would otherwise be discarded.
External linksStructure / PubMed:34048698
MethodsEM (single particle)
Resolution2.3 - 3.7 Å
Structure data

EMDB-30199:
Cryo-EM reconstruction of PEGylated full-length NOD2
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-30200:
Cryo-EM reconstruction of equine apoferritin (unmodified)
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-30202:
Cryo-EM reconstruction of equine apoferritin (1 mM PEG4)
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-30203:
Cryo-EM reconstruction of equine apoferritin (4 mM PEG4)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-30204:
Cryo-EM reconstruction of equine apoferritin (1 mM PEG8)
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-30205:
Cryo-EM reconstruction of equine apoferritin (4 mM PEG8)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-30206:
Cryo-EM reconstruction of E.coli beta-galactosidase (unmodified)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-30207:
Cryo-EM reconstruction of E.coli beta-galactosidase (2 mM PEG4)
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-30208:
Cryo-EM reconstruction of E.coli beta-galactosidase (2 mM PEG8)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-30404:
Cryo-EM reconstruction of PEGylated tetrameric ADH
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-30405:
Cryo-EM reconstruction of PEGylated tetrameric beta-amylase
Method: EM (single particle) / Resolution: 2.3 Å

Source
  • Oryctolagus cuniculus (rabbit)
  • Equus caballus (horse)
  • Escherichia coli (E. coli)
  • Saccharomyces cerevisiae (brewer's yeast)
  • Ipomoea batatas (sweet potato)

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