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TitleCryo-EM Structure of Phospholipase Ce Reveals Roles for the N-terminal Domains in Maximum Activity
Journal, issue, pagesTo Be Published
Publish dateMar 12, 2024 (structure data deposition date)
AuthorsSamassekou K / Lyon AM
External linksSearch PubMed
MethodsEM (single particle)
Resolution3.8 - 4.28 Å
Structure data

44064

9b13

EMDB-44064, PDB-9b13:
Cryo-EM structure of phospholipase Cepsilon PH-COOH in complex with an antigen-binding fragment (composite structure)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-44065: Cryo-EM structure of phospholipase Cepsilon PH-COOH in complex with an antigen-binding fragment (consensus map)
Method: EM (single particle) / Resolution: 3.87 Å

EMDB-44066: Cryo-EM structure of phospholipase Cepsilon PH-COOH in complex with an antigen-binding fragment (focused map)
Method: EM (single particle) / Resolution: 4.28 Å

EMDB-44067: Cryo-EM structure of phospholipase Cepsilon PH-COOH in complex with an antigen-binding fragment (focused map)
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / phospholipase c / antigen-binding fragment / complex

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