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TitleSingle particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 2386, Year 2019
Publish dateJun 3, 2019
AuthorsXiao Fan / Jia Wang / Xing Zhang / Zi Yang / Jin-Can Zhang / Lingyun Zhao / Hai-Lin Peng / Jianlin Lei / Hong-Wei Wang /
PubMed AbstractThe fast development of single-particle cryogenic electron microscopy (cryo-EM) has made it more feasible to obtain the 3D structure of well-behaved macromolecules with a molecular weight higher than ...The fast development of single-particle cryogenic electron microscopy (cryo-EM) has made it more feasible to obtain the 3D structure of well-behaved macromolecules with a molecular weight higher than 300 kDa at ~3 Å resolution. However, it remains a challenge to obtain the high-resolution structures of molecules smaller than 200 kDa using single-particle cryo-EM. In this work, we apply the Cs-corrector-VPP-coupled cryo-EM to study the 52 kDa streptavidin (SA) protein supported on a thin layer of graphene and embedded in vitreous ice. We are able to solve both the apo-SA and biotin-bound SA structures at near-atomic resolution using single-particle cryo-EM. We demonstrate that the method has the potential to determine the structures of molecules as small as 39 kDa.
External linksNat Commun / PubMed:31160591 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.3 Å
Structure data

0689

6j6j

EMDB-0689: The reconstruction of biotin-bound streptavidin at 3.2 Angstrom resolution
PDB-6j6j: Biotin-bound streptavidin
Method: EM (single particle) / Resolution: 3.2 Å

0690

6j6k

EMDB-0690: The reconstruction of apo-state streptavidin at 3.3 Angstrom resolution
PDB-6j6k: Apo-state streptavidin
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-BTN:
BIOTIN

ChemComp-HOH:
WATER

Source
  • streptomyces avidinii (bacteria)
KeywordsCYTOSOLIC PROTEIN / streptavidin

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