Single particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 31160591.
- Also identified by DOI 10.1038/s41467-019-10368-w and PMC identifier 6546690.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
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.
Medical subject headings
- Biotin
- Cryoelectron Microscopy
- Single Molecule Imaging
- Streptavidin